1
Course Syllabus and Lesson Plan
SCID 141
Living Processes: From Molecules to Cells
(Chemical processes in living system)...
2
Evaluation of Student Achievement
Grading system from midterm and final examination
• Midterm written examination (MCQ) ...
3
Course Syllabus and Lesson Plan
SCID 142
Laboratory in Living Processes
Academic Year 2012-2013: 23 November 2012 – 11 F...
4
Teaching Methods:
Laboratory, Group study, Discussion and assignment
1. Laboratories: Compulsory
There are 3 laboratory ...
5
Evaluation of student achievement:
Grading system from written examination and work assignments or performance in the
ac...
6
SCID 141-142 6
RA, BM, PI
-
12 . . 55 8.30-10.20
Course Orientation
Lecture 1: Structure and Functions of Biomolecules
a...
7
-
Lab 2: Determination of Liver Enzyme Activities –
Brief Lab
all OP-
(BC), (BC), (BC),
(BC), (BC), (BC),
(BC), (BC), an...
8
SC1-139, SC1-141, SC1-220, SC1-221, SC1-321, SC1-322, SC2-133, SC2-134, SC2-136,
SC2-139, SC2-140, SC2-142, SC2-222, SC2...
9
LESSON PLAN
Lecture 1: Structure and Function of Biomolecules
Instructor: Kittisak, Biochemistry Faculty of Science
Date...
10
2. Nucleotides and Nucleic Acids
2.1 Basic properties of nucleotides & nucleic acids Chapter 8, page 273-279
2.2 Nuclei...
11
LESSON PLAN
Lecture 2: Protein Structure and Concept of Folding
Instructor: Jirundon, Biochemistry, Faculty of Science
...
12
LESSON PLAN
Lecture 3: Biocatalysis and Enzyme Kinetics
Instructor: Kittisak, Biochemistry, Faculty of Science
Date/Tim...
13
3.3 Factors facilitating catalysis in Chymotrypsin
4. Regulatory Enzymes
4.1 Feedback inhibition
4.2 Covalent modificat...
14
LESSON PLAN
Lecture 4: Protein Structure and Function/ Molecular Assembly
Instructor: Jirundon, Biochemistry, Faculty o...
15
LESSON PLAN
Lecture 5: Citric Acid Cycle and Oxidative Phosphorylation
Instructor: Tuangporn, Biochemistry, Faculty of ...
16
Leading questions:
Fate of pyruvate
1. In anaerobic condition or insufficient of O2 to be used in tissue, what is the f...
17
3. Study from the course textbook
References:
1. Lehninger Principle of Biochemistry 4th edition, 2005
Part II Bioenerg...
18
LESSON PLAN
Laboratory 1: Enzyme LDH
Lab Coordinator: Kittisak, Biochemistry, Faculty of Science
Date/Time: Friday, 23 ...
19
LESSON PLAN
Lecture 6: Carbohydrate Metabolism
Instructor: Wilai, Biochemistry, Faculty of Science
Date/Time: Monday, 2...
20
Gluconeogenesis
1. Why do we need to synthesized glucose de novo? (P. 543)
2. What are precursors of glucose in glucone...
21
LESSON PLAN
Lecture 7: Amino Acids Metabolism
Instructor: Wilai, Biochemistry, Faculty of Science
Date/Time: Wednesday,...
22
11.List cofactor/coenzyme involve in one carbon transfer? How it is related to amino acid
/nucleotide metabolism?
12.Wh...
23
LESSON PLAN
PBL: Hunger Strike
Tutors: Staffs
Scenario Organizers: Assoc. Prof. Wilai Noonpakdee, Biochemistry, Faculty...
24
LESSON PLAN
Lecture 8: Nucleotide Metabolism
Instructor: Tuangporn, Biochemistry Faculty of Science
Date/Time: Friday, ...
25
References:
• Chapters 21-22 of Nelson, D. L., and Cox, M. M., Lehninger Principles of Biochemistry, 4th
edition, W. H....
26
LESSON PLAN
Lecture 9: Nutritions
Instructor: Wilai, Biochemistry, Faculty of Science
Date/Time: Wednesday, 12 December...
27
LESSON PLAN
Small Group Conference 1: Structure and Functions of Hemoglobin
Conference Coordinator: Kittisak, Biochemis...
28
8. During early development, the human fetus expresses different α and β hemoglobin genes. These
are similar but not id...
29
LESSON PLAN
Lecture 10: Lipid Metabolism
Instructor: Jamorn, Biochemistry, Faculty of Science
Date/Time: Monday, 17 Dec...
30
What is the source (form) of electron used for reduction reactions in fatty acid biosynthesis?
(P.792, fig 21-5)
What i...
31
LESSON PLAN
Lecture 10: Heme and Minerals Metabolism
Instructor: Jamorn, Biochemistry, Faculty of Science
Date/Time: We...
32
LESSON PLAN
Tutorial 1: Structure, Kinetics and Metabolism
Tutorial Staffs: Jamorn, Jirundon, Kittisak, Tuangporn, Bioc...
33
LESSON PLAN
Lecture 12: Integration and Regulation of Metabolism
Instructors: Jamorn, Biochemistry, Faculty of Science
...
34
LESSON PLAN
Laboratory 2: Determination of Liver Enzyme Activities
Lab Coordinator: Tuangporn, Biochemistry, Faculty of...
35
LESSON PLAN
Small Group Conference 2: Active Learning Lesson Diabetes
Conference Coordinator: Jamorn, Biochemistry, Fac...
36
LESSON PLAN
Lecture 13: Xenobiotic Biotransformation
Instructor: Krongtong, Pharmacology, Faculty of Science
Date/Time:...
37
LESSON PLAN
Lecture 14: Pharmacogenomics and Clinical Correlation
Instructor: Krongtong, Pharmacology, Faculty of Scien...
38
LESSON PLAN
Laboratory 3: Determination of Serum lipid
Lab Coordinator: Jamorn, Biochemistry, Faculty of Science
Date/T...
39
LESSON PLAN
Lecture 15: Food toxicology
Instructor: Somchai, Pharmacology, Faculty of Science
Date/Time: Monday, 21 Jan...
40
LESSON PLAN
Lecture 17: Gene and Chromosome Structure
Instructor: Sarawut, Biochemistry, Faculty of Science
Date/Time: ...
41
3. Study from the course textbook
Learning Materials provided:
• List of suggested readings.
Student Assessment:
Multip...
42
LESSON PLAN
Lecture 18: DNA Replication Repair and Recombination
Instructor: Sarawut, Biochemistry, Faculty of Science,...
43
- How does tRNAs carry amino acids?
- What is the function of peptidyl transferase?
- Why does protein synthesis consum...
44
LESSON PLAN
Lecture 19: Gene Expression and Regulation
Instructor:: Sumalee, Biochemistry, Faculty of Science
Date/Time...
45
• What are the „inducer‟ of Lac Operon ? What are the roles of lactose, allolactose and IPTG in
regulating Lac Operon ?...
46
LESSON PLAN
Lecture 20: DNA Technology
Instructor: Sumalee, Biochemistry, Faculty of Science
Date/Time: Wednesday, 30 J...
47
LESSON PLAN
Laboratory 4: DNA Isolation, PCR and Gel electrophoresis
Lab Coordinator: Sumalee, Biochemistry, Faculty of...
48
LESSON PLAN
Small Group Conference 3: Molecular Technology in Medicine
Conference Coordinator: Sumalee, Biochemistry, F...
49
LESSON PLAN
CAI: Molecular Diagnostic, PCR and DNA Sequencing
Coordinator: Sumalee, Biochemistry, Faculty of Science
Da...
50
LESSON PLAN
Lecture 21: Biochemistry knowledge and medicine
Instructor: Jamorn, Biochemistry, Faculty of Science
Date/T...
51
LESSON PLAN
TBL 1: Metabolic Syndrome
TBL Staffs: Apirom and Team, Pathology, Faculty of Medicine Ramathibodi Hospital
...
52
LESSON PLAN
Tutorial 2: Metabolic Integration and Nutrition
Tutorial Staffs: Jamorn, Tuangporn, Wilai, Biochemistry, Fa...
53
LESSON PLAN
Tutorial 3: Genetics and DNA Technology
Tutorial Staffs: Sarawut, Sumalee, Biochemistry, Faculty of Science...
54
LESSON PLAN
Tutorial 4: Xenobiotic and Drug Metabolism
Tutorial Staffs: Krongtong, Somchai, Pharmacology, Faculty of Sc...
55
Small Group Conferences
small group conferences PBL
PBL 7 -
Conference Group PBL Group Number
1 1 & 2
2 3 & 4
3 5 & 6
4...
56
PBL Hunger Strike
Meeting 1
Section I
30 November 2012, 13:30-16:20
Section II
3 December 2012, 8:30-10:20
(BC) SC1-139...
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57
PBL 1 5
Group :I PI-PBL 1-8, BM PBL 9-14, Group II RA PBL 15-28
PBL 1
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2 5522006
3 5522017
3 5522022
5 5522...
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PBL 3
1 5522005
2 5522012
4 5522033
4 5522039
5 5522043 *
6 5522057
7 5522068
8 5522075 *
9 5522081
10 5522099
12 55...
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59
PBL 5
1 5522009
2 5522021
3 5522029
4 5522042
5 5522048
6 5522060
7 5522071
8 5522084
9 5522086
10 5522106 *
11 5522...
60
60
PBL 7
1 5522011
2 5522027
3 5522031
4 5522045
5 5522052
6 5522066
7 5522073
8 5522090
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11 552211...
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PBL 9
1 5514001
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PBL 11
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PBL 13
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PBL 15
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PBL 21
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SCID
5 6
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  1. 1. 1 Course Syllabus and Lesson Plan SCID 141 Living Processes: From Molecules to Cells (Chemical processes in living system) Academic Year 2012-2013: 12 November 2012 – 18 Febuary 2013 Course Title: Living Processes, From Molecules to Cells Course Code: SCID 141 Total Credit: 3(3-0) Pre-Requisite: SCBI 101, SCBI 102, SCBI 103, SCBI 104 Duration: Second semester - -- Course Homepage: http://www.sc.mahidol.ac.th/scbc/webboard/index.php Course Description: Structures and functions of biomolecules, protein folding, protein functions, bio-catalysis, enzyme kinetics, citric acid cycle, electron transport and oxidative phosphorylation, anabolism and catabolism of biomolecules in normal and some important pathological stages, regulation of metabolic pathways, flow of genetic information, gene regulation, and molecular techniques with medical applications. Course Objectives: At the end of this course, the students will be able to 1. explain chemical processes occurred in living system, structure and functional relationship of biomolecules 2. point out the regulation of metabolic pathways governing the life of a cell 3. know and understand energy metabolism, biosynthesis and degradation in both normal and some important pathological stages 4. emphasize fundamental of genome organization, flow of genetic information and gene regulation 5. learn the principle of molecular techniques relevant to medical applications. Course Outlines: See schedule on page Teaching Methods Lecture, Group study, Tutorial and assignment Teaching Media • Text book Lehninger, Principle of Biochemistry, 4th or 5th edition, • CAI, VDO, PowerPoint and/or transparency presentation, can be self-study via web site: http://www.sc.mahidol.ac.th/scbc/webboard/index.php
  2. 2. 2 Evaluation of Student Achievement Grading system from midterm and final examination • Midterm written examination (MCQ) 30% • Final written examination (MCQ) 70% Total 100% Students who get a total grade more than 50% are considered successful for this course. Course Evaluation Questionnaire about contents, teaching processes, examinations and instructor performance. Required Textbook • Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 4th or 5th edition, Worth, New York Other References 1. Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990. 2. John, W. Baynes and Marek H. Dominiczak, Medical Biochemistry, 2nd edition, Elsevier Mosby, 2005 3. Other equivalent biochemistry textbooks. Instructors Lecturer from Department of Biochemistry, Pharmacology, Physiology and Clinician and guest lecturers from outside Faculty of Science Course Coordinators Asist. Prof. Dr. Jamorn Somana Department of Biochemistry, Faculty of Science, Mahidol University Tel: 0-2201-5601 and 0-2201-5468
  3. 3. 3 Course Syllabus and Lesson Plan SCID 142 Laboratory in Living Processes Academic Year 2012-2013: 23 November 2012 – 11 Febuary 2013 Course Title: Laboratory in Living Processes Course Code: SCID 142 Total Credit: 1(0-3) Pre-Requisite: SCBI 101, SCBI 102, SCBI 103, SCBI 104, SCID141 Duration: Second semester Course Homepage: http://www.sc.mahidol.ac.th/scbc/webboard/index.php Course Description: Determination of LDH enzyme activity by spectrophotometric method, Determination of liver enzyme activities, DNA isolation and PCR amplification followed with analysis of DNA by gel electrophoresis technique, structures and functions of biomolecules, protein folding, protein functions, bio-catalysis, enzyme kinetics, TCA cycle, electron transport and oxidative phosphorylation, anabolism and catabolism of biomolecules in normal and pathological stages, regulation of metabolic pathways, flow of genetic information, gene regulation, and molecular techniques with medical applications. Starvation LDH Course Objectives: At the end of this course, the students will be able to 1. have a laboratories skill on basic techniques in structure and functional relationship of biomolecules 2. gain the knowledge and understand the way to analysis the experimental data 3. work together or have group activities relevant to chemical processes occurred in living system and medical applications 4. acquire necessary knowledge through current available resources and analyze critical problems and data obtained. Course Outlines: See schedule on page
  4. 4. 4 Teaching Methods: Laboratory, Group study, Discussion and assignment 1. Laboratories: Compulsory There are 3 laboratory exercises designed to broaden the students‟ skill and knowledge. These are 1) determination of LDH enzyme activity and studying LDH enzyme kinetics by spectrophotometric method 2) determination of liver enzyme activities 3) DNA isolation, PCR amplification and analysis of DNA by gel electrophoresis technique. 2. Small Group or Conferences: Compulsory There are 3 small group discussions. The sessions involve discussion on problem sets related to the topics SCID 141 and some clinical cases. Student presentation and discussion will be focused and all sessions will have either pre- or post discussion quizzes. 3. Problem-Based Learning: Compulsory Problem-based scenario will be given to initiate group activities in the discussion and self-study sessions to find out a possible explanation for the problem. Developments of conceptual thinking skill and integration of information are the main objective. 4. Team-Based Learning: Compulsory There is 1 team-based learning topic given to initiate group activities in the learning processes. Students have to study the assignment topics before a class. Questions involved in the topics will be asked and the students have to find out the answers individually then try to find out within their group. Developments of conceptual thinking by him- or her-self and by group with integration of information are the major objective of this learning. 5. Tutorials: Not Compulsory There are 3 tutorial periods to cover the basic concepts of the course. Tutorial period is provided to help students better understand the topics and/or clarify some points after their self- or group-study. Therefore, students are expected to go through the topics and prepare questions prior to each tutorial discussion. Questions for each tutorial session can be posted at the web-board (see course homepage) or can be submitted directly to the lecturer(s). All tutorials will be held at lecture hall. 6. CAI (CD and VDO): Compulsory There are 1 CAI media available in this course, i.e. structure folding and build block, high throughput automated system, and molecular diagnosis, PCR and sequencing technique. These learning materials will be installed in the computer system and the students can access and study during free time. One CAI-media on PCR and DNA sequencing techniques is used in a class discussion. Teaching Media: • Laboratory manual of the course • Text book Lehninger, Principle of Biochemistry, 4th or 5th edition, • CAI, VDO, PowerPoint and transparency presentations, can be self study via web site: http://www.sc.mahidol.ac.th/scbc/webboard/index.php
  5. 5. 5 Evaluation of student achievement: Grading system from written examination and work assignments or performance in the activities Process 85% Small group (5% x3), pre- or post-test (5%x3) 30% PBL (10% x 2) 20% Laboratories (5% x 4) 20% CAI (5%) 5% TBL iRad 5% tRad 2.5% gRad 2.5% 10% Knowledge 15% From written examination (Midterm and Final) Out of the total 100%, students who get a grade more than 60% are considered successful for this course Course Evaluation: Questionnaire about contents, teaching processes, examinations and Instructor performance. Required Textbook • Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 4th or 5th edition, Worth, New York Other References: 1. Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990. 2. John, W. Baynes and Marek H. Dominiczak, Medical Biochemistry, 2nd edition, Elsevier Mosby, 2005 3. Other equivalent biochemistry textbooks. Instructors: Lecturer from Department of Biochemistry, Pharmacology, Physiology and Clinician from Ramathibodi and guest lecturers from outside Faculty of Science. Course Coordinators: Asist. Prof. Dr. Jamorn Somana Department of Biochemistry, Faculty of Science, Mahidol University Tel: 0-2201-5601 and 0-2201-5468
  6. 6. 6 SCID 141-142 6 RA, BM, PI - 12 . . 55 8.30-10.20 Course Orientation Lecture 1: Structure and Functions of Biomolecules all OP- (BC), (BC) 14 10.30-12.20 Lecture 2: Protein Structure and Concept of Folding all OP- (BC) Lecture 3: Biocatalysis and Enzyme Kinetics all OP-- (BC) 19 8.30-10.20 Lecture Protein Structure and Function / Molecular Assembly all OP- (BC) 21 10.30-12.20 Lecture 5: Citric Acid Cycle / Oxidative Phosphorylation all OP- (BC) 23 Lab 1: Enzyme LDH – Brief Lab all OP-- (BC), (BC), (BC), (BC), (BC), (BC), (BC) and TAsLab 1: Enzyme LDH – Experiment all SC3- 6 8.30-10.20 Lecture 6: Carbohydrate Metabolism all OP- (BC) 8 10 2 Lecture 7 Amino Acid Metabolism all OP- (BC)- PBL Hunger Strike Meeting /1 PBL Section I SC1/SC2 (BC), (BC), (BC), (BC), (BC), (BC), (PM), (PS), (RA) (PM), (PM), (), (AN) and TAs - - PBL Hunger Strike Meeting /2 PBL Section II SC1/SC2 (BC), (BC), (BC), (BC), (BC), (BC), (PM), (PS), (RA) (RA), (PM), (PM), () (BC) and TAs Lecture 8: Nucleotide Metabolism all OP- (BC)- Lecture 9: Nutrition all OP- (BC)- - Conference 1: Hemoglobin Structure and Function all SC1/SC2 (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC), (IMB), (IMB) and TAs - Lecture 10: : Lipid Metabolism Nutrition all OP- (BC) 10.30-12.20 Lecture 1: Heme and Mineral Metabolism all OP- (BC) - Tutorial 1: Q&A Structure, Kinetics and Metabolism all OP- (BC), (BC), (BC), (BC) 24-28 5 31 55-1 56 - Lecture 12: Integration and Regulation of Metabolism all OP- (BC)
  7. 7. 7 - Lab 2: Determination of Liver Enzyme Activities – Brief Lab all OP- (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC), and TAs - Lab 2: Determination of Liver Enzyme Activities – Experiment all SC3 - Conference 2: Active Learning Lesson: Diabetes all OP- (BC), (BC), (BC), (BC), (BC), , (BC), (BC), (BC), (BC), (BC), (PM), ( (PS), (RA), and TAs Lecture 13: Xenobiotic Biotransformation all OP- (PM)- - PBL: Hunger Strike Meeting 2/1 PBL Section I SC1/SC2 (BC), (BC), (BC), (BC), (BC), (BC), (PM), (PS), (RA) (RA), (PM), (PM), (BC), (BC) and TAs - PBL: Hunger Strike Meeting 2/2 PBL Section II SC1/SC2 (BC), (BC), (BC), (BC), (BC), (BC), (PM), (PS), (RA) (RA), (PM), (PM), (PS), (BC) and TAs 10.30-12.20 Lecture 14: Pharmacogenomics and Clinical Correlation all OP- (PM) 13.30-14.30 Lab 3: Determination of Serum Lipids – Brief Lab all OP- (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC) and TAs14.30-16.20 Lab 3: Determination of Serum Lipids – Experiment all SC3 - Lecture 15: Food Toxicology all OP- (PM) 10.30-12.20 Lecture 17: Gene and Chromosome Structure all OP- (BC) - Lecture 18: DNA Replication Repair and Recombination all OP- (BC) Lecture 19: Gene Expression and Regulation all OP- (BC) 10.30-12.20 Lecture 20: DNA Technology all OP- (BC) 13.30-14.30 Lab 4: DNA Isolation, PCR, Electrophoresis – Brief Lab all OP- (BC), (BC), (BC), (BC), (BC), (BC), (BC) (BC), and TAs14.30-16.20 Lab 4: DNA Isolation, PCR, Electrophoresis – Experiment all SC3 - Conference 3: Molecular Technology in Medicine all SC1/SC2 (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC), (BC), (IBM) (IMB), (IMB) and TAs 10.30-12.20 CAI: Molecular Diagnostic, PCR and DNA Sequencing all OP- (BC) and team - Lecture 21: Biochemistry Knowledge and Medicine all OP- (BC) - TBL 1: Metabolic Syndrome all OP- (RA), (RA), (RA), (RA), (RA), (RA), (BC) and TAs 10.30-12.20 Tutorial 2: Q&A Metabolism all OP- (BC), (BC), (BC) - Tutorial 3: Q&A Gene and DNA Technology all OP- (BC), (BC) - Tutorial 4: Xenobiotic and Drug Metabolism all OP- (PM), (PM) –
  8. 8. 8 SC1-139, SC1-141, SC1-220, SC1-221, SC1-321, SC1-322, SC2-133, SC2-134, SC2-136, SC2-139, SC2-140, SC2-142, SC2-222, SC2-322
  9. 9. 9 LESSON PLAN Lecture 1: Structure and Function of Biomolecules Instructor: Kittisak, Biochemistry Faculty of Science Date/Time: Monday, 12 November 2012, 8:30-10:20 Room: OP- Learning Objectives: At the end of this lecture, students will be able to 1. Carbohydrates and Glycobiology 1.1 identify the structure and characteristics of common carbohydrates 1.2 differentiate various classes of carbohydrate and their functions 1.3 discuss on the major carbohydrate components of extracellular matrices 1.4 differentiate storage and structural carbohydrates in animal and plant 2. Nucleotides and Nucleic Acids 2.1. understand basic structures of nucleotides, DNA, RNA and derivatives 2.2. differentiate various types/structures of nucleic acids 2.3. discuss basic chemistry of nucleic acids 2.4. discuss various functions of nucleotides 3. Lipids 3.1 understand basic structure and chemical properties of lipids 3.2 discuss on the chemistry and structures of membrane-forming lipids 3.3 discuss roles of lipids 4. Biological Membranes and Transports 4.1. discuss on biological membrane composition and architecture 4.2. understand dynamics of lipid-bilayer membranes 4.3. discuss on transport of substances across biological membranes Reference: • Lehninger Principles of Biochemistry by Nelson and Cox, 4th Edition 2005 Content Outlines: 1. Carbohydrates and Glycobiology 1.1 Monosaccharides and disaccharides Chapter 7, page 238-246 1.2 Polysaccharides Chapter 7, page 247-255 1.3 Glycoconjugates: proteoglycans, Chapter 7, page 255-261 glycoproteins and glycolipids 1.4 Carbohydrates as informational molecules Chapter 7, page 261-267 Leading Questions: • What is the difference between aldose and ketose sugars? (P. 239) • What is the difference between D and L sugar? (P. 240) • What are the different isoforms/derivatives of glucose and their biological significance? (P. 241-244) • What are reducing sugars and how do you test for it? (P. 244-245) • What are the major storage polysaccharides in nature? What are they composed of? (P. 247- 248) • Which carbohydrates are components of extracellular matrix that serves as lubricants in joints of vertebrates? (253-254) • What are lectins and how do they involved with carbohydrate molecules? (P. 262-267)
  10. 10. 10 2. Nucleotides and Nucleic Acids 2.1 Basic properties of nucleotides & nucleic acids Chapter 8, page 273-279 2.2 Nucleic Acid Structure Chapter 8, page 279-291 2.3 Nucleic acid chemistry Chapter 8, page 291-300 2.4 Other functions of nucleotides Chapter 8, page 300-302 Leading Questions: • What are the different types of nucleotides and their common names? (P. 273-275) • What are major groove and minor groove in the DNA structure? (P. 282) • What are the differences between DNA and RNA? • Why is DNA more stable than RNA? • How does UV light cause DNA damage? (P. 694-695) • Besides being a building block of nucleic acids, what are other functions of nucleotides? (P. 300-302) 3. Lipids 3.1 Storage lipids Chapter 10, page 343-348 3.2 Structural lipid in membranes Chapter 10, page 348-357 3.3 Lipids as signals, cofactors, and pigments Chapter 10, page 357-363 Leading Questions: • What are fatty acids and how do they differ from one another? (P. 343-344) • What are triglycerides and waxes? What are their roles in nature? (P. 345-348) • What are the different types of membrane-forming lipids? (P. 348-350) • What is the role of membrane lipids in blood group determination? (P. 354) • What are sterols? Give some examples of their derivatives. (P. 354-355, 359) • What are eicosanoids and what are their roles? (P. 358-359) 4. Biological Membranes and Transports 4.1 Composition and architecture of membranes Chapter 11, page 369-380 4.2 Membrane dynamics Chapter 11, page 380-389 4.3 Solute transport across membranes Chapter 11, page 389-416 Leading Questions: • How biological membranes are formed from lipid molecules? (P. 370-373) • How do different proteins associate with lipid-bilayer membranes? (P. 373-376) • What are examples of plasma membrane proteins involved in membrane surface adhesion? (P. 385-386) • What are the different types of solute transport across biological membranes? (P. 389-393) • What is the role of GLUT4 protein in the removal of blood sugar? (P. 396) • How are Na+ and K+ transported across the lipid membranes? (P. 398-399) Learning Organization: • Lecture is given • Students review and study the learning materials according to the outlined content Learning Materials provided: • Lehninger Principles of Biochemistry by Nelson and Cox, 4th Edition 2005 • Slide presentation provided on the web site Student Assessment: • Self-assessments are provided on the web or at the end of each chapter. • MCQ with short explanation exam
  11. 11. 11 LESSON PLAN Lecture 2: Protein Structure and Concept of Folding Instructor: Jirundon, Biochemistry, Faculty of Science Date/Time: Wednesday, 14 November 2012, 10:30-12:20 Room: OP- Learning Objectives: Students are able to • describe unique properties of water that are crucial for properties, structural assembly, and functions of macromolecules and thus for a living system. • differentiate various types of chemical interactions in aqueous solution. • describe general features of amino acids as building blocks of proteins. • recognize chemical properties of amino acids whose chemical structures are given. • describe the general concept of formation of protein 3D structure and chemical interactions involved. • describe importance of weak-force interactions in protein folding. • recognize importance of water in protein folding. Content Outlines: • Chemical interactions in aqueous solution. • Proteins as major components of cells. • Proteins are polymers of amino acids. • Natural amino acids with diverse chemical properties. • Hierarchy of protein 3D structure. • Importance of weak-force interactions in protein folding. Learning Organization: • The session consists of a three-hour lecture using PowerPoint presentation that aims to give students overview and basic concept about protein structure and amino acids, as well as weak-forced interaction involved in protein structure stabilization and folding. • Students are encouraged to read a textbook for more information about protein structure and amino acids. Learning Materials provided: • Hand-out of PowerPoint presentation. References: • Amino Acid Quiz (http://info.bio.cmu.edu/Courses/BiochemMols/PQuiz/PQInst.html) • Chapter on protein and amino acids in any new biochemistry textbook such as (but not limited to): • Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 2nd edition, Worth, New York, 1993. • Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990. • Branden, C., and Tooze, J., Introduction to Protein Structure, Garland, New York, 1991. Student Assessment: • Multiple-choice questions with short (written) explanations.
  12. 12. 12 LESSON PLAN Lecture 3: Biocatalysis and Enzyme Kinetics Instructor: Kittisak, Biochemistry, Faculty of Science Date/Time: Friday, 19 November 2012, 13:30-16:20 Room: OP- Learning Objectives: Student will be able to 1. Introduction to Enzymes 1.1. explain basic and common properties of enzymes. 1.2. describe thermodynamics of reactions catalyzed by enzymes and compare to the reactions without catalysis. 1.3. describe factors specifying enzyme active site and specificity. 1.4. describe types of reactions catalyzed by enzymes 1.5. explain concepts and roles of cofactors in catalysis 2. Introduction to Enzyme Kinetics 2.1. describe a plot of initial rates versus substrate concentrations 2.2. derive the initial rate equation according to the Michaelis-Menten model. 2.3. use graphical methods to calculate Km, Vmax, kcat, kcat/Km and explain the meanings of these parameters. 2.4. explain different types of enzyme inhibition. 3. Example of Enzyme Catalysis 1.1 describe hydrolysis of a peptide bond without catalysis by proteases. 1.2 write reaction mechanism of Chymotrypsin-catalyzed reactions 1.3 describe factors facilitating catalysis in Chymotrypsin 4. Regulatory Enzymes 4.1. explain feedback inhibition. 4.2. describe the role of covalent modification in controlling catalysis. 4.3. explain functional roles of allosteric enzymes. 4.4. describe functions of zymogen or proenzymes. Content Outline 1. Introduction to Enzymes 1.1 What is enzyme? 1.2 Thermodynamics of reactions catalyzed by enzymes 1.3 Enzyme active site and specificity 1.4 Types of reactions catalyzed by enzymes 1.2 Cofactor 2. Introduction to Enzyme Kinetics 2.1 A plot of initial rates versus substrate concentrations 2.2 Derivation of Michaelis-Menten model 2.3 Km, Vmax, kcat, kcat/Km 2.4 Enzyme inhibition 3. Example of Enzyme Catalysis 3.1 Hydrolysis of a peptide bond 3.2 Mechanism of Chymotrypsin-catalyzed reactions
  13. 13. 13 3.3 Factors facilitating catalysis in Chymotrypsin 4. Regulatory Enzymes 4.1 Feedback inhibition 4.2 Covalent modification 4.3 Allosteric enzymes 4.4 Zymogen or proenzymes Learning Organization: 1. Lecture 120 min. 2. Q&A 10 min. 3. Study from the course textbook References: • Lehninger Principle of Biochemistry 4th edition, 2005 Chapter 6 Enzymes • Biochemistry by Berg, Tymoczko, and Stryer, 6th Edition, 2006 Chapter 8-9 Student Assessment: Multiple-choice questions with short (written) explanations.
  14. 14. 14 LESSON PLAN Lecture 4: Protein Structure and Function/ Molecular Assembly Instructor: Jirundon, Biochemistry, Faculty of Science Date/Time: Monday, 19 November 2012, 8:30–10:20 Room: OP- Learning Objectives: Students will be able to • differentiate various types of chemical interactions in aqueous solution. • describe importance of weak-force interactions in assembly of biomolecules. • recognize importance of water in molecular assembly. • distinguish specific recognition from non-specific binding. Content Outlines: • Various types of molecular assembly.  Non-specific binding.  Specific recognition. • Cellular compartmentalization and fluid mosaic membrane structure. • Chemical interactions involved in assembly of biomolecules by examples.  Ion channel.  Chaperone. Learning Organization: • The session consists of a two-hour lecture using PowerPoint presentation that aims to give students overview and basic concept about biomolecular assembly. • Students are encouraged to read the provided material and any textbook for more information about molecular assembly and various complexes of biomolecules. Learning Materials provided: • Hand-out of PowerPoint presentation. References: • Chapters on biomolecular complexes and membrane-associated proteins in any new biochemistry textbook such as (but not limited to): • Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 2nd edition, Worth, New York, 1993. • Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990. Student Assessment: Multiple-choice questions with short (written) explanations.
  15. 15. 15 LESSON PLAN Lecture 5: Citric Acid Cycle and Oxidative Phosphorylation Instructor: Tuangporn, Biochemistry, Faculty of Science Date/Time: Wednesday, 21 November 2012, 10.30-12.20 Room: OP- Learning Objectives: Student will be able to 1. Introduction to metabolism 1.1. discuss thermodynamic functions (ΔG) and the meaning of spontaneous change and equilibrium. 1.2. explain free energy change upon ATP hydrolysis and role of ATP as energy currency. 1.3. discuss the concept of high energy biomolecules and their roles in coupled reactions and other biological processes. 1.4. explain the concept of oxidation-reduction reaction, half reactions, reduction potential and the use of coenzymes as electron carriers in biological system. 1.5. recognize the importance of flow of electron in the redox reaction to provide energy for doing biological work. 1.6. define catabolism and anabolism. 2. Fate of pyruvate, citric acid cycle, electron transport and oxidative phosphorylation 2.1. describe fates of the pyruvate under aerobic and anaerobic conditions. 2.2. outline citric acid cycle (TCA or Krebs‟ cycle) and discuss its function in the oxidation of acetate and production of electrons. 2.3. explain the process of electron transfer in mitochrondria to regenerate of oxidized coenzyme and to produce proton gradient from energy of this electron transfer. 2.4. discuss the coupling in oxidative phosphorylation (role of ATP synthase in transformation of energy from proton gradient into ATP synthesis). 2.5. compare and contrast oxidative phosphorylation and substrate level phosphorylation. 2.6. discuss the effects of uncouplers and electron transport inhibitors. Lecture Outlines: 1. Introduction to metabolism 1.1. Therodynamics, concepts of equilibrium, Gibbs free energy, and energy transformation in biological systems 1.2. Phosphoryl group transfers, role of ATP and coupling reaction 1.3. Oxidation-reduction reactions:- half-reaction, reduction potential, biological redox reaction, flow of electron in biological work, coenzymes as electron carriers 1.4. Energy metabolism: anabolism/catabolism 2. Fate of pyruvate, citric acid cycle, electron transport and oxidative phosphorylation 2.1. Fate of pyruvate in aerobic and anaerobic conditions 2.2. Citric acid cycle:- oxidation of acetate to carbon dioxide, electron production 2.3. Regulation of citric acid cycle; by allosteric property of pyruvate dehydrogenase complex, and three exogonic steps 2.4. The importance of intermediates in citric acid cycle in anabolism 2.5. Electron transfer in mitochrondria: component in electron transport chain, regeneration of oxidized coenzyme and electron flow, inhibitors 2.6. Coupling of electron transport and oxidative phosphorylation: proton gradient, ATP synthase, 2.7. Effects of uncouplers and electron transport inhibitors
  16. 16. 16 Leading questions: Fate of pyruvate 1. In anaerobic condition or insufficient of O2 to be used in tissue, what is the fate of pyruvate, why does it happen that way and how do tissues reuse it when O2 consumption becomes sufficient? (P. 538) 2. What is the role of a derivative of vitamin B1, thiamine pyrophosphate, in formation of acetyl-CoA? (P. 540-541) Citric acid cycle 1. What are the three major stages of cellular respiration? (P 601) 2. Pyruvate dehydrogenase complex is a cluster of three enzymes and five cofactors. What types of reaction does it catalyse? Write down the overall reaction and explain the function of each cofactor. (P 602 and P 605 or summary 16.1 P 606) 3. What is the net reaction of citric acid cycle? How many GTP and reduced electron carriers are produced from 1 acetyl CoA? In which organelle does the reaction occur? (P 607) 4. Write down the following reactions in the citric acid cycle:- condensation, decarboxylation, oxidation reduction and substrate-level phosphorylation reactions, What are the forms of energy produced from this complete oxidation of acetyl CoA. (P 606-607) 5. Intermediates in the citric acid cycle can be used for anabolic pathway. How these intermediated are replenished? (P 616-618) What is/are the role(s) of biotin in those processes? (P 618) 6. Can intermediates in citric acid cycle such as Succinyl CoA be used to synthesis glucose? How? (P 617, Fig 16-15; P 543-544, P548) 7. How is citric acid cycle regulated? (P621, 16.3 first paragraph; and P 623, Summary) Electron transport chain and Oxidative phosphorylation 1. In electron transport chain what is the terminal electron acceptor molecule and what is the final product? (P 690) 2. What are the differences between oxidative phosphorylation and substrate level phosphorylation (P 690, P 531) 3. Write down the series of electron transfer starting from NADH to the terminal electron acceptor. How does this order of electron transfer related to the redox potential of each electron carrier? (P 694-696) 4. Where is the complex I to IV localized? What are their functions in electron transport chain? (P 696) 5. Concerning electron transport chain, what is “Proton gradient” or “Electrochemical potential”? Where does the gradient occur in animal cell? How does electron transfer generate proton gradient? What is its significance? (P 701) 6. In oxidative phosphorylation, how is ATP synthesized? What is the energy driving the synthesis of ATP? (P 704-707) 7. What does “Coupling” in oxidative phosphorylation refer to? (P 704-705 Fig 19-18) 8. What is “Respiratory uncoupler” Give one example of uncoupler and its mechanism of action (p705, p707) 9. Why is cyanide or carbonmonoxide highly toxic? (P 696 fig 19-6, P 705) 10. How can DNP lead to overheat production in the cell? (P 705, P 707) Learning Organization: 1. Lecture 100 min. 2. Q&A 10 min.
  17. 17. 17 3. Study from the course textbook References: 1. Lehninger Principle of Biochemistry 4th edition, 2005 Part II Bioenergetics and Metabolism (P.481-488) Chapter 15 Principles of Bioenergetics Chapter 16 The Citric Acid Cycle Chapter 19 Oxidative Phosphorylation 2. multimedia in http://www.wiley.com/legacy/college/boyer/0470003790/animations/animations.htm :Citric acid cycle and Cori cycle 3. http://cbag2.sc.mahidol.ac.th/bc_intranet/th/course_schdule/SCID221/index.php :ATP synthase (Ed Wood) Student Assessment: Multiple-choice questions with short (written) explanations.
  18. 18. 18 LESSON PLAN Laboratory 1: Enzyme LDH Lab Coordinator: Kittisak, Biochemistry, Faculty of Science Date/Time: Friday, 23 November 2012, 13:30-16:20 Room: OP- , MDL SC3-304, 308, 404, 408 Learning Objectives: Student should be able to 1. measure enzyme activity that is a specific property of enzyme. 2. calculate the the Km and Vmax values that are the characteristic of each enzyme. 3. explain the isoenzymes efficiency in different organs using the Km and Vmax values. Content Outlines: 1. Determination of bovine late dehydrogenase (H4) enzyme activity 2. Determination of Km and Vmax of the LDH (H4) by Lineweave-Burk plot Learning Organization: 1. Studying the laboratory manual provided in advance. 2. Lab preview 30 min, OP- . 3. Pre-test or homework to prepare a flow chart. 4. Hand on laboratory experiment. 5. Laboratory discussion Learning Materials Provided: 1. Laboratory manual 2. Chemicals, equipments for laboratory test. References: 1. Laboratory manual 2. Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 2nd edition, Worth, New York, 1993. 3. Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990. Student Assessment: For processes evaluation: 5% of total score per lab • Quiz or pre-test and Attendance 30% • Report (by Group) 40% • Post test (Lab discussion) 30%
  19. 19. 19 LESSON PLAN Lecture 6: Carbohydrate Metabolism Instructor: Wilai, Biochemistry, Faculty of Science Date/Time: Monday, 26 November 2012, 8:30-10:20 Room: OP- Learning Objectives: Students should be able to 1. define catabolism and anabolism and discuss their relationship. 2. describe the two basic phases of the breakdown of glucose into two molecules of pyruvate, structural specificity and key regulating steps. 3. differentiate fates of the pyruvate in glycolysis under aerobic and anaerobic conditions. 4. compare the opposing pathway of glycolysis and gluconeogenesis and the body needs to regulate glucose level. 5. identify functional points in the body to oxidize glucose in pentose phosphate pathway and cause of damage when this pathway is limited. 6. discuss storage and reusing of carbohydrate in animal cells form glycogen and cause of a common pathological sign in glycogen storage diseases. Content Outlines: 1. Catabolism and anabolism and their relationship 2. Two phases of glycolysis pathways, energy gain and key regulatory steps. 3. Fates of pyruvate in aerobic and anerobic conditions. 4. Regulation of free glucose level in the body via gluconeogenesis. 5. Roles of pentose phosphate pathway in generating and usage of NADPH and effect of G6PD. 6. Glucose strorage and reuse from glycogen, its pathway and some defects which cause glycogen storage disease. Leading Questions: Glycolysis 1. Why do cells principally need D-glucose not other forms of sugar? (see structure (P. 243) 2. What is the principle of cells to make sugar to be entered in metabolic pathway in the form of phosphate sugar? (P. 525) 3. How do sugars change from aldose to ketose or one epimer to another epimer? (P. 527) 4. How does fructose 1,6 biphosphate change from 1C6 to 2C3? (P. 527-529) 5. What are three irreversible steps in glycolysis and what is the significance of these reactions? (P 544, P575) 6. What products do cells get from glycolysis and what cells will do to these products?(P. 533, 899) 7. How do human take various types of carbohydrate to be used as glucose phosphate or fructose phosphate? (P. 534) 8. In anaerobic or insufficient of O2 to be used in tissue, what is the fate of pyruvate, why does it happen that way and how do tissues reuse it when O2 consumption becomes sufficient? (P. 538) 9. What is the role of a derivative of vitamin B1, thiamine pyrophosphate, in formation of acetyl-CoA? (P. 540-541) 10.Why do many adult Asian people get diarrhea after drinking fresh milk? 11.Km of glucokinase in liver and hexokinase in muscle are different? How does this difference play role in function of liver and muscle concerning intake of glucose to cell? (P 576-578)
  20. 20. 20 Gluconeogenesis 1. Why do we need to synthesized glucose de novo? (P. 543) 2. What are precursors of glucose in gluconeogenesis? (P. 544) 3. What is the role of biotin in oxaloacetate formation? (P. 546) 4. In animal, can acetyl-CoA be used in gluconeogenesis, if not, why/ if yes, how? (P 548) 5. Why gluconeogenesis and glycolysis cannot take place simultaneously? (P 548-549) 6. Why liver but not muscle is the major organs to generate glucose into bloodsteam? (P-547) Pentose phosphate pathway 1. Why do animal cells need to do glucose oxidation? (P. 550, 552) 2. What is the functional difference between NADH and NADPH? (P. 549) 3. How do cells synthesize other carbon numbered sugar from hexose such as ribose and what is the role of thiamine pyrophosphate here? (P. 552) 4. Why does G6PD cause haemolysis in some certain conditions? (P. 551) Glycogen synthesis and degradation 1. Why extension sides of glucopolysaccharides in the cell are C4 or C6 ends (nonreducing ends)? 2. How is α 1,6 glycosidic bond of glycogen formed and brokendown? (P. 563) 3. Why does polysaccharide synthesis within the cell need sugar monomer in a form of C1 sugar nucleotide for example, UDP-glucose for glycogen synthesis? (P. 565) 4. Why does glycogen break down generate glucose-1-phosphate without using ATP and how does the product change to glucose-6-phosphate (P. 564) 5. Why do most glycogen storage diseases cause hepatomegaly (enlarge liver)? (P. 567) 6. Explain terms: glycogenolysis, glycolysis, glycogen synthesis and gluconeogenesis. (P 562) Learning Organization: 1. Lecture 160 min. 2. Q&A 10 min. 3. Study from the course textbook References: Lehninger: Chapter 14, 15 (2 Chapters only), Student Assessment: Multiple-choice questions with short (written) explanations.
  21. 21. 21 LESSON PLAN Lecture 7: Amino Acids Metabolism Instructor: Wilai, Biochemistry, Faculty of Science Date/Time: Wednesday, 28 November 2012, 10:30-12:20 Room: OP- Learning Objectives: Students will be able to 1. describe metabolic fate of amino groups (p657-665) 2. explain urea cycle, its control and its role in the nitrogen excretion.The role of special enzymes glutamine synthetase and glutamate dehydrogenase in the nitrogen preservation in our body. 3. discuss pathways of amino acid degradation (in general) 4. describe some diseases causing by defects in amino acid metabolism(677, 679-685) 5. explain how we can synthesize some amino acids (non essentials) (841) and important molecules that derived from them (854-61) Content Outline: 1. Metabolic fate of amino groups: degradation of protein to amino acid, amino group transfer and release as ammonia, transportation of ammonia to hepatic tissues. (657-65) 2. Nitrogen excretion and the urea cycle: how urea is formed in liver, krebs bicycle, urea cycle regulation, genetic defect in urea cycle. (665-70) 3. Amino acid degradation: ketogenic vs glucogenic amino acid, vitamin and cofactors involved. (671-75) 4. Some genetic disorders (metabolic diseases) affecting amino acid catabolism. (677-85) 5. Amino acid biosynthesis and its regulation. (841, 851-53), 6. Molecules derived from amino acid. (854-61) Leading Questions: 1. How does nitrogen in amine group transfer from one compound to another and how is it eliminated from the body? (p 657-58) 2. What is the role of vitamin B6 in the amino acid metabolism? (660-2) 3. Explain the link between urea and Kreb‟s cycle, list enzymes and coumpounds involved in, where does it occur in the cell and why do we have to produce urea instead of other nitrogenous waste? (666-9,671) 4. What is the waste composition in urea molecule and where do these molecule come from? Why it is dangerous if intake only protein diet and vitamins to lose weight? 5. Why certain amino acid should be restricted in diabetic patient? 6. What are the functions of Alanine transaminase (ALT) and aspartate transaminase (AST)? Why does ALT have the highest activity of all the mammalian liver aminotransferase? (667) What are the roles of these two enzyme as diagnostic tool? (664) 7. Why some amino acids are considered to be essential and what are they? 8. Some genetic diseases in amino acid metabolism are quite unique and occasionally appear such as albinism, phenylketouria, alkaptouria, maple syrup urine disease and argininosuccinic academia. Which defective enzymes are they, what are accumulated intermediates and how to reduce those toxic intermediate in general? (p667) 9. Patients who has genetic defect in phenylalanine hydroxylase need tyrosine which is normally nonessential amino acid, why? What is/are the excreted products that cause phenylketouria in these patients? 10.What is Methyl malonyl CoA acidimia? How it is related to amino acid degradation?
  22. 22. 22 11.List cofactor/coenzyme involve in one carbon transfer? How it is related to amino acid /nucleotide metabolism? 12.Which amino acid is the precursor of these substances: dopamine, adrenaline, norepinehprine, tyroxine, glutathione, porphyrin, GABA, histamine, nitric oxide? (p.860-1) Learning Organization: 1. Lecture 160 min. 2. Q&A 10 min. 3. Study from the course textbook Learning Materials Provided: • Slides from PowerPoint lecture presentation References: • Chapters 21-22 of Nelson, D. L., and Cox, M. M., Lehninger Principles of Biochemistry, 4th edition, W. H. Freeman and Company, New York, 2005 or comparable chapters in other text books. Student Assessment: Multiple-choice questions with short (written) explanations.
  23. 23. 23 LESSON PLAN PBL: Hunger Strike Tutors: Staffs Scenario Organizers: Assoc. Prof. Wilai Noonpakdee, Biochemistry, Faculty of Science Date/Time: 1st Meeting: Section 1: Friday, 30 November 2012, 13:30-16:20 Section 2: Monday, 3 December 2012, 8:30-10:20 2nd Meeting: Section 1: Friday, 11 January 2013, 13:30-16:20 Section 2: Monday, 14 January 2013, 8:30-10:20 Room: SC1-139, SC1-141, SC1-220, SC1-221, SC1-321, SC1-322, SC2-133, SC2-134, SC2-136, SC2-139, SC2-140, SC2-142, SC2-222, SC2-322 Learning Objectives: Students should be able to use the active learning method to 1. describe the effect of food deprivation on metabolism and discuss the mechanisms by which the body attempts to maintain blood glucose level. 2. appreciate the concepts of metabolic specialization and fuel preferences of individual tissues. 3. discuss the processes involved in nitrogen homeostasis. 4. discuss the critical role of ketone bodies during starvation. 5. describe the consequences of prolonged deficiency of micronutrients. Learning Outlines: A case scenario of a man on hunger strike, brought to a hospital by his wife. Problems, medical history, physical examination and laboratory investigation are included. Learning Organization: 1. A scenario is provided at least one week in advance to the students and tutors. 2. A written tutorial guide on the case is provided in advance to the tutors who will facilitate the active learning process of the students. 3. Students are divided into 28 groups; each group contains 10-13 students. A tutor is assigned for each PBL group. Students will have two 2-hr meeting sessions. 4. The first session allows the students to use critical thinking and relevant discussions to formulate the learning objectives. 5. Students carry out independent study on the assigned learning objectives by using a variety of information resources. 6. In the second meeting session in the following week, students report their findings to the group, and through exchanging ideas and discussions, formulate the hypothesis and draw conclusion. Learning Materials: 1. A case scenario. 2. Textbooks and material resources relevant to the problem. Assessment: by students and tutors 1. Performance (identifying, solving problems, active learning and presentation). 2. PBL test at the end of the course.
  24. 24. 24 LESSON PLAN Lecture 8: Nucleotide Metabolism Instructor: Tuangporn, Biochemistry Faculty of Science Date/Time: Friday, 7 December 2012, 13:30-16:20 Room: OP- Learning objectives: The student should be able to 1. explain 2 distinct biosynthesis pathways of purines and pyrimidines (de novo and salvage pathway). 2. explain the degradation pathway of purine and pyrimidine nucleotides. 3. list some diseases caused by metabolic disorder of purine and pyrimidine metabolism. 4. explain how purines and pyrimidines metabolic pathway can be used to develop chemotherapeutic agents. Content outlines: 1. Biosynthesis of nucleotides and its regulation: de novo: purines (862-66) pyrimidines (866- 72), salvage pathway (875) 2. Degradation of purines and pyrimidines (873-75) 3. Diseases caused by defect in nucleotide biosynthesis and degradation pathway, i.e. gout, lesh-nyhan, ADA deficiency (873-5) 4. Chemotherapeutic drug target in thymidylate and folate metabolism (876-77) Leading Questions: 1. What are the differences between de novo and salvage pathway biosynthesis of nucleotides? 2. What amino acid can be precursor in de novo synthesis of both purines and pyrimidines? 3. How deoxyribonucleotides are made from ribonucleotides? What are the roles of thioredoxin and glutathione in these reactions(869-71) 4. How does one carbon group transfer from one compound to another and how does it link to methionine, cysteine synthesis, vitamin B12 and folic? (P. 672-674, 845) 5. What are functions of ribonucleotide in the cell beside the building box of RNA? 6. What is the reason to have methyl group for dTMP in DNA but not for UMP in RNA? 7. What are differences between de novo and salvage pathway? 8. How does human body excrete and control amount of uric? (P. 874-875) 9. How different between gout and Lesch Nyhan syndrome? (P. 875) 10.Why some food such as poultry, entrails, young vegetable shoot and fermented food are not suitable for gout patients? 11.Allopurinol is a drug to treat gout, what is the mechanism of this compound?(876) 12.We normally don‟t degrade nucleotides to produce energy as compare to carbohydrate, fat and protein? What evidence or observations should you think it would be? 13.List anticancer drugs that target enzymes involving in nucleotides metabolism 14.What the differences between Gout and Lesh Nyhan syndrome? Why Lesh Nyhan syndrome patients also develop gout or hyperuricimia? Learning Organization: 1. Lecture 100 min. 2. Q&A 10 min. 3. Study from the course textbook Learning Materials Provided: • Slides from PowerPoint lecture presentation
  25. 25. 25 References: • Chapters 21-22 of Nelson, D. L., and Cox, M. M., Lehninger Principles of Biochemistry, 4th edition, W. H. Freeman and Company, New York, 2005 or comparable chapters in other text books. Student Assessment: Multiple-choice questions with short (written) explanations.
  26. 26. 26 LESSON PLAN Lecture 9: Nutritions Instructor: Wilai, Biochemistry, Faculty of Science Date/Time: Wednesday, 12 December 2012, 10:30-12:20 Room: OP- Learning Objectives: Students should be able to 1. describe the role and functions of the six classes of dietary nutrients. 2. assess the nutritional status across life span including calories, essential nutrients, protein, fat, carbohydrate needed. 3. list some major health problems that can be related to unhealthy food intake, eating disorders (bulimia, anorexia nervosa, obesity, under nutrition). 4. recognize vitamins structures and explain their functions and derivatives of medical important requirements, deficiency and/or toxicities. 5. describe mineral requirements, their deficiency and toxicities. Content outline: 1. Nutrients: 6 classes of nutrients, macro and micro nutrients and their functions 2. Energy balance: calories needed per day related to nutrients 3. Vitamins structure and functions, their toxicities, and deficiency symptoms: water soluble and fat soluble vitamins 4. Minerals: major vs. trace elements : their functions and deficiency symptoms 5. Health problems related to unhealthy food intake Leading Questions: 1. What is macro and micro nutrient? 2. Which of the vitamins would most likely become deficient in a vegetarian person? 3. What are the structures of the vitamin B1 , B6 and B12? 4. What is the function of vitamin K in relation to blood clotting? 5. What is WERNICKE-KORSAKOFF SYNDROME? 6. Which is the form of vitamin D in our body? 7. A Thai infant presents with prominent forehead, bowing of the limbs, broad and tender wrists, and irritability. Which of the vitamins is recommended? 8. Define the term; BMI, Calorie, and RDA. 9. Is it true that taking calcium supplement during menopause will increase bone mass and prevent osteoporosis? Learning Organization: 1. Lecture 100 min. 2. Q&A 10 min. Reference: • Baynes, J.W. and Dominiczak, M.H., Medical Biochemistry, 2nd edition, Elsevier 2005 Student Assessment: Multiple-choice questions with short (written) explanations.
  27. 27. 27 LESSON PLAN Small Group Conference 1: Structure and Functions of Hemoglobin Conference Coordinator: Kittisak, Biochemistry, Faculty of Science Date/Time: Friday, 14 December 2012, 13:30–16:30 Room: SC1-139, SC1-141, SC1-220, SC1-221, SC1-321, SC1-322, SC2-133, SC2-134, SC2-136, SC2-139, SC2-140, SC2-142, SC2-222, SC2-322 Learning Objectives: Students will be able to 2. discuss their understanding of hemoglobin structure how it functions 3. integrate and understand basic concepts learned from Lecture 1 - 4 on structure and function relationship of biomolecules 4. apply basic physical concept to understand biochemical processes Learning Materials: Part 1 • Conference questions are assigned to students. • Each students study the assigned question and present their answer in front of the class Part 2 • Students are assigned a post test to quiz their understanding of the material of the conference and the tutorial 1 and 2 Reference: • Lehninger Principles of Biochemistry by Nelson and Cox, 4th Edition 2005 page 157 - 174 Conference Content: Hemoglobin is one of many molecules that comprise erythrocytes (red blood cells) and give them their ability to bind and transport oxygen to and from the many different tissues of the body. In this part of the conference, we will discuss structurally how hemoglobin performs its function. Questions: 1. Compare and contrast the structure of hemoglobin and myoglobin. What are the differences and similarities between the two proteins in terms of structure and function? 2. Discuss the cooperative binding of oxygen by hemoglobin A. What are the T state and R state? 3. Explain how CO2 is transported from tissues to lung. 4. What is the Bohr Effect? How is it related to the T and R states of the hemoglobin? 5. CO2 transport by the red blood cell in tissues is usually accompanied by a change in pH. The pH change can affect the amino acid side chains in protein differently due to different in individual‟s pKa value(s). Explain the meaning of pKa. 6. Histidine is an amino acid with 3 pKa values of 2, 6 and 9, respectively. What is the net charge of histidine at pH 1.5, 5, 7, and 10? 7. Explain how BPG is involved in human adaptation to high altitude.
  28. 28. 28 8. During early development, the human fetus expresses different α and β hemoglobin genes. These are similar but not identical to the hemoglobin genes expressed in adults. This fetal hemoglobin is less sensitive to BPG than the adult hemoglobin. As a result, fetal hemoglobin has a higher affinity for oxygen, allowing transfer from the maternal adult hemoglobin. The structural difference between the fetal and adult hemoglobin is that the amino acid residue 143 of the β chain in adult hemoglobin is histidine while that of the fetal hemoglobin is serine. Discuss how this single amino acid difference contributes to different sensitivity to BPG. 9. What is the effect of each of the following treatments on the oxygen affinity of hemoglobin A? (a) Increase pH from 7.2 – 7.4 (b) Increase pCO2 from 10 – 40 torrs (c) Increase concentration of BPG from 2x10-4 – 8x10-4 M (d) Dissociation of α2β2 into monomeric subunits 10.Explain how sickle-cell anemia is caused. What goes wrong with the hemoglobin of patient with such disease?
  29. 29. 29 LESSON PLAN Lecture 10: Lipid Metabolism Instructor: Jamorn, Biochemistry, Faculty of Science Date/Time: Monday, 17 December 2012, 8:30-10:20 Room: OP- Learning Objectives: Student will be able to 1. explain digestion, mobilization and transport of fats. 2. describe utilization and storage of energy in lipid form, generation of ATP from fatty acids and ketone bodies 3. identify similarities and differences between fatty acid oxidation and fatty acid synthesis and control of fatty acid oxidation and biosynthesis Content Outlines: 1. Absorption and transportation of dietary fat in the body and lipoproteins 2. Regulation of fatty acid oxidation and biosynthesis 4. Ketone bodies generation and usage 5. Essential fatty acid and ecosanoid compounds which are linked NSAID Leading Questions Fatty acid catabolism Why lipid (triglyceride) is more suitable as storage fuels compare to carbohydrate? (P.631, 346) How does lipid transport from intestine to target tissues? How do apolipoproteins and lipase involve in this process? (P. 632-633) What is the effect of glucagon on lipid metabolism in adipose tissue? (P.634) What is the role of carnitine and coenzyme A in fatty acid degradation? (P.635-636 Fig 17-6) What is the rate limiting step (regulatory step) in fatty acid oxidation? (P.636) Write down four repeated reactions of beta-oxidation and their products. (P.637-638, Fig 17-8) How do human oxidize cis form of unsaturated fatty acid? (637-639 Fig 17-8&17-9) What is the function of Acyl CoA dehydrogenase? What would be the effect of Acyl CoA deficiency? (P.638, 643 Fig 17-8) Besides normal coenzymes required for general beta-oxidation, what are coenzymes/cofactors required for oxidation of odd-number fatty acid? What are their functions? (P.642 fig 17-11) What is the effect of excess glucose on regulation of fatty acid oxidation? (P.642-643) What are ketone bodies and how do they generated? (P.650-652) Lipid biosynthesis How does biosynthesis of fatty acids differ from their breakdown? (P. 787-791) How is malonyl-CoA involved in fatty acid biosynthesis? (P.787) What is the coenzyme help in catalyzing carboxylation reaction by acting as CO2 carrier and transfer CO2 to organic substrate? (P.788) Which is the first fatty acid formed by the fatty acid biosynthesis process and how it is formed? (P. 791-793) Where is the fatty acid biosynthesis taken place? How does the substrate for this process transported to that site? (P.794-795) How does acyl group bind to fatty acid synthase? (P.790)
  30. 30. 30 What is the source (form) of electron used for reduction reactions in fatty acid biosynthesis? (P.792, fig 21-5) What is the rate limiting step for fatty acid synthesis? (P.795-796) How insulin, glucagon and fatty acyl CoA level regulate fatty acid biosynthesis? (P.796-797, fig 21-11) Can mammalian cells synthesize polyunsaturated fatty acids such as linolenic acid? Why is polyunsaturated fatty acid necessary for our body? (P.800) Fatty acids are substrates for synthesis of variety of signaling molecules in a family of eicosanoids such as prostaglandins, thromboxane. What are the fatty acid substrate and the key enzymes for synthesis these compounds? (P.800-801) What is the role of certain drugs like aspirin and ibuprofen? (P. 800-801) What are the common processes in the biosynthesis of both triacylglycerols and glycerophospholipids? (P. 804) How is heart disease related to cholesterol, how it is initiated? (P. 827) What are VLDL, LDL, HDL and chylomicron? How do they differ from one another? (P. 820- 824) How do cells get rid of plasma LDL particles? (P. 824-825) Many drugs for treatment of hypercholesterolemia, such as lovastatin, act on inhibiting cholesterol synthesis by inhibiting enzyme at the rate-limiting step. What is the rate-limiting step in the synthesis of cholesterol? How hormone and cholesterol level regulate cholesterol synthesis? (P.825-826, p827) Learning Organization: 1. Lecture 100 min. 2. Q&A 10 min. 3. Study from the course textbook References: • Lehninger Principle of Biochemistry 4th edition, 2005 Student Assessment: Multiple-choice questions with short (written) explanations.
  31. 31. 31 LESSON PLAN Lecture 10: Heme and Minerals Metabolism Instructor: Jamorn, Biochemistry, Faculty of Science Date/Time: Wednesday, 19 December 2012, 10:30-12:20 Room: OP- Learning Objectives: Students will be able to 1. describe how heme is synthesized, degraded and eliminated from the body. 2. dxplain some clinical conditions which are connected to abnormal heme metabolism. 3. describe the special chemical properties of some minerals in biochemical reactions. 4. explain how the body take up, maintain and modify some minerals. Content Outlines: 1. Tetrapyrrole synthesis for heme and its degradation 2. Porphyria and hyperbillirubinemia 3. Special chemical properties of some minerals such as Fe, Co, Cu, P, S and I. 4. Biochemical reactions and metabolic pathways which link to some minerals Leading Questions: Heme Metabolism 1. What are precursors and the first committed intermediate of porphyrins synthesis? (P. 855) 2. What is the significant difference in term of structure between preuroporphyrinogen (uroporphyrinogen I) and uroporphyrinogen III? (P. 855) 3. Why many pyrrole compounds are phototoxic? 4. What is the function of haem in haemoproteins? (P. 158, 693) 5. Why does high level of haemolysis cause jaundice and how does the body cope with this condition? (P. 856) 6. Why our serum urine and feces have yellowish-brown colour? Do those colours come from the same compound? (P. 856) 7. What is enterohepatic circulation? 8. Why do many porphyrias coincide with anemia? (P.857) Mineral Metabolism 1. Why is calcium deposited in the bone? 2. What are the roles of phosphate in biomolecules? 3. How iron is able to carry oxygen in hemoglobin or transfer electron in cytochromes. 4. What is the special property of cobalt in methylmalonyl-CoA mutase? 5. What is Wilson disease? How does it link to copper metabolism? 6. What are the roles of sulfur compounds in carbohydrate and protein structures? 7. Why does iodine need to be cation before integrated into tyroxine? Learning Organization: • Lecture • Questions and answers Learning Materials Provided: • Slides from PowerPoint lecture presentation References: • Chapters 21-22 of Nelson, D. L., and Cox, M. M., Lehninger Principles of Biochemistry, 4th edition, W. H. Freeman and Company, New York, 2005 or comparable chapters in other text books. Student Assessment: Multiple-choice questions with short (written) explanations.
  32. 32. 32 LESSON PLAN Tutorial 1: Structure, Kinetics and Metabolism Tutorial Staffs: Jamorn, Jirundon, Kittisak, Tuangporn, Biochemistry, Faculty of Science Date/Time: Tuesday, 27 January 2012, 8:30-10:20 Room: OP- Learning Objectives: Students should be able to 1. raise questions regarding the lecture topics not understood to tutorial instructors. 2. spend the time in the tutorial to clarify lecture contents. Learning organization: 1. Students study the learning materials in advance according to the outline content and questions for students to answer after they study the content. 2. Students post any questions regarding the tutorial content prior to or at the tutorial session. 3. Questions are answered and explained at the tutorial session.
  33. 33. 33 LESSON PLAN Lecture 12: Integration and Regulation of Metabolism Instructors: Jamorn, Biochemistry, Faculty of Science Date/Time: Wednesday, 2 January 2013, 10:30-12:20 Room: OP- Learning Objectives: Students will be able to understand metabolism and functions, hormones functions and mechanisms, hormones and control of metabolism, regulations of metabolism, metabolic integration in the coordinated and orderly functions of the organs, and the physiological biochemistry on body functions. Content Outlines: 1. Metabolism 1.1 Metabolic junction intermediates and inter tissue transferring of intermediates. 1.2 Metabolism and the metabolic pathways localization or compartmentalization in cells and tissues (organs). 1.3 Bioenergetics and metabolism, the relationship of catabolic and anabolic processes in cell (organ) functions. 2. Metabolic regulations and hormone 2.1 Metabolic changes in each organ in response to hormones. 2.2 Hormones classification based on the functions and mechanisms of the actions. 2.4 Medical endocrinology, hormones and analogs (drugs) in the control for the orderly and coordinated functions of the cells, tissues and the organs (body functions). Learning Organization: 1. Lecture 100 min. 2. Q&A 10 min. 3. Study from the course textbook References: A. Lehninger Principles of Biochemistry; Nelson and Cox, 4th Edition, 2005. (Good standard text and very informative for good backgrounds, but maybe a bit too detailed for readings?) B. Biochemistry; The National Medical Series for Independent Study (NMS, USA); Davidson and Sittman, 4th Edition, 1999. (Supplement reading for discussion on the relevant clinical aspects).
  34. 34. 34 LESSON PLAN Laboratory 2: Determination of Liver Enzyme Activities Lab Coordinator: Tuangporn, Biochemistry, Faculty of Science Date/Time: Friday, 4 January 2013, 13:30-16:20 Room: OP- , MDL SC3-304, 308, 404, 408 Learning Objectives: Student should be able to 1. Perform basic biochemical assay to test activities of liver enzymes, AST and ALT, from serum sample. 2. Interpret the assay results. Content Outlines: 1. Determination of serum ALT activities in serum 2. Determination of serum AST activities in serum Learning Organization: 1. Studying the laboratory manual provided in advance. 2. Lab preview 30 min, OP- . 3. Pre-test or homework to prepare a flow chart. 4. Hand on laboratory experiment. 5. Laboratory discussion Learning Materials Provided: 1. Laboratory manual 2. Chemicals, equipments for laboratory test. References: 1. Laboratory manual 2. Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 2nd edition, Worth, New York, 1993. 3. Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990. Student Assessment: For processes evaluation: 5% of total score per lab • Quiz or pre-test and Attendance 30% • Report (by Group) 40% • Post test (Lab discussion) 30%
  35. 35. 35 LESSON PLAN Small Group Conference 2: Active Learning Lesson Diabetes Conference Coordinator: Jamorn, Biochemistry, Faculty of Science Date /Time: Monday, 7 January 2013, 08:30-10:20 Room: SC1-139, SC1-141, SC1-220, SC1-221, SC1-321, SC1-322, SC2-133, SC2-134, SC2-136, SC2-139, SC2-140, SC2-142, SC2-222, SC2-322 Learning Objectives: Students will be able to 1. Extend your basic knowledge about diabetes to further details. 2. Compare and contrast points of basic differences in terms of biochemical and physiological parameters in diabetic and normal people 3. Catch information from the example case and integrate the concept map Learning Materials: Part 1 • Slide of yes or no questions as a Bingo game • Description slides to clarify further necessary concepts Part 2 • Case example for analysis • Questions and answers • Writing a concept map Reference: • Lehninger Principles of Biochemistry by Nelson and Cox, 4th Edition 2005 page 157 - 174 Student Assessment: Class participation and concept map
  36. 36. 36 LESSON PLAN Lecture 13: Xenobiotic Biotransformation Instructor: Krongtong, Pharmacology, Faculty of Science Date/Time: Wednesday, 9 January 2013, 10:30-12:20 Room: OP- Learning Objectives: Students are able to 1. list the fundamental concepts of xenobiotic biotransformation as determinants of drug and xenobiotic action, adverse reactions and toxicity 2. describe the process of biotransformation of xenobiotics 3. describe how the knowledge of xenobiotic biotransformation help explain and predict the onset, duration, severity of toxicity and pathogenesis of exposure to xenobiotics. Outline • Define: Xenobiotic (Drug) metabolism, bioactivation, activation, detoxification • The consequence of biotransformation: the drug, drug action, drug effect, drug interaction, drug toxicity • Phase I and phase II xenobiotic biotransformation • Xenobiotic biotransformation as a determinant of the pharmacological action of drugs, adverse drug reaction and biological response • Determinants of rate of biotransformation: Molecular aspect: enzyme induction, enzyme inhibition Suggested Reading Topics: http://web.vet.cornell.edu/public/pharmacokinetics/sitesDT/frame_sitesDT.html References: Katzung, B.C. (2007) Basis and Clinical Pharmacology, 10th ed. Lange Medical Books/McGraw-Hill Companies Goodman & Gilman‟s (2006) The pharmacological Basis of Therapeutics, 11th ed. The McGraw-Hill Companies, Inc. Learning Organization: Studying the learning materials provided in advance 1. Lecture 100 min 2. Questions and answers 10 min Learning Materials provided: • An assigned chapter • List of suggested readings Student Assessment: Multiple-choice questions with short (written) explanations.
  37. 37. 37 LESSON PLAN Lecture 14: Pharmacogenomics and Clinical Correlation Instructor: Krongtong, Pharmacology, Faculty of Science Date/Time: Wednesday, 16 January 2013, 10:30-12:20 Room: OP- Learning Objectives: Students are able to 1. define terms: Pharmacogenomics, drugs efficacy, drugs safety, genotype and drug response 2. explain why it is believed that understanding an individual's genetic makeup is the key to creating personalized drugs with greater efficacy and safety. 3. describe how pharmacogenomics could affect the way medicine is practiced 4. list the benefits of pharmacogenomics Lecture Outline: 1. Pharmacogenomics: What is it? 2. The anticipated benefits of pharmacogenomics 3. Is pharmacogenomics in use today? 4. What are some of the barriers to pharmacogenomics progress? 5. A five-step pharmacogenomic approach for a new drug, successively taking into account the genes involved in: ▪ pharmacokinetics (absorption, distribution, metabolism, transport) ▪ pharmacodynamic phase ▪ specific disorders and related metabolic pathways deviations ▪ biological variability in genes responses including their physiological regulation ▪ environmental effects. 6. Issues applicable:enzymes involved in the metabolism of xenobiotics and the receptors and other gene-product targets for drugs 7. Screening for bioavailability and potential drug-drug interactions. 8. Toxicogenomics -the application of pharmacogenomics principles to issues of predictive toxicity. 9. Prediction of risk of cancer and other diseases caused by environmental chemicals and physical agents that individuals are inadvertently exposed to Suggested Reading Topics: Principles of drug action http://www.ama-assn.org/ama/pub/category/2306.html References: • Katzung, B.C. (2007) Basis and Clinical Pharmacology, 10th ed. Lange Medical Books/McGraw-Hill Companies • Goodman & Gilman‟s (2006) The pharmacological Basis of Therapeutics, 11th ed. The McGraw-Hill Companies, Inc. Learning Organization: • Students study the learning materials in advance according to the outlined content • Core concepts will be discussed in class Learning Materials provided: List of suggested readings. Student Assessment: • Self-assessments are provided • MCQ with short explanation exam
  38. 38. 38 LESSON PLAN Laboratory 3: Determination of Serum lipid Lab Coordinator: Jamorn, Biochemistry, Faculty of Science Date/Time: Friday, 18 January 2013, 13:30-16:20 Room: OP- , MDL SC3-304, 308, 404, 408 Learning Objectives: Student should be able 1. To familiarize biochemical and enzymatic assays for determination of triglyceride and cholesterol 2. To be able to evaluate serum lipid status and correlate to clinical interpretation Content Outlines: 1. Determine serum total cholesterol 2. Determine serum total triglycerides 3. From the provided HDL-cholesterol values determine LDL-cholesterol 4. Calculate atherogenic index Learning Organization: 1. Studying the laboratory manual provided in advance. 2. Lab preview 30 min, OP- . 3. Pre-test or homework to prepare a flow chart. 4. Hand on laboratory experiment. 5. Laboratory discussion Learning Materials Provided: 1. Laboratory manual 2. Chemicals, equipments for laboratory test. References: 1. Laboratory manual 2. Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 2nd edition, Worth, New York, 1993. 3. Allain CC et al. Enzymatic determination of total serum cholesterol. Clin Chem. 1974; 20: 470-475. 4. Mgowan MW et al. A peroxidase couple method for the colorimetric determination of serum triglycerides. Clin Chem. 1983; 29: 538-542. 5. Friedewald WT. Estimation of concentration of low-density lipoprotein cholesterol in plasma, without use of the preparative ultracentrifuge, Cli Chem. 1972; 18: 499-502. 6. Gill PI et al. Regulation of acyl Co A: Cholesterol acyl transferase activity in normal and atherotic aortas: Role of a cholesterol substrate pool. Exp Mol pathol. 1986; 44: 320-329. Student Assessment: For processes evaluation: 5% of total score per lab • Quiz or pre-test or Attendance 30% • Report (by Group) 40% • Post test (Lab discussion) 30%
  39. 39. 39 LESSON PLAN Lecture 15: Food toxicology Instructor: Somchai, Pharmacology, Faculty of Science Date/Time: Monday, 21 January 2013, 8:30-10:20 Room: OP- Learning objectives 1. Identify signs and symptoms of food poisoning. 2. Identify factors that influence the severity of food poisoning. 3. Classify common food-borne diseases in Thailand 4. Classify common food contaminants in Thailand Content outline 1. Definition of food toxicology 2. Signs and symptoms of food poisoning 3. Factors influencing the severity of food poisoning 4. Food-borne diseases 5. Food contaminants Learning organization 1. Studying the learning materials provided in advance 2. Lecture 130 min 3. Questions and answers 30 min 4. Self study of the following topics Learning Material provided 1. Slides from powerpoint lecture presentation Student Assessment: • Self-assessments are provided • MCQ with short explanation exam
  40. 40. 40 LESSON PLAN Lecture 17: Gene and Chromosome Structure Instructor: Sarawut, Biochemistry, Faculty of Science Date/Time: Wednesday, 23 January 2012, 10:30-12:20 Room: OP- Learning Objectives: Students should be able to Gene, genome and chromosome 1. describe the meanings of gene, genome and chromosome 2. discuss the organization of prokaryotic and eukaryotic genes DNA metabolism 1. list factors required for DNA replication 2. explain the functions of enzymes and protein in DNA replication 3. define the meanings of leading and lagging strand DNA synthesis, and okazaki fragment 4. explain the concepts of mutation and repair mechanism Content Outlines: 1. Gene, genome and chromosome 1.1 Higher structure of DNA in prokaryote and eukaryote Chapter 24, p923-32 1.2 Typical structure of prokaryote and eukaryote gene Chapter 24, p938-45 1.3 Nuclear and organelle encoded genes Chapter 19, p719-20 1.4 Coding and non-coding sequences Chapter 24, p928-30 Leading questions: - What are gene, genome and chromosome defined? - What is the component of nucleosome? - What are the differences between prokaryotic and eukaryotic genes? - Where are the coding and non-coding DNA sequences found? 2. DNA metabolism 2.1 Flow of genetic material, the central dogma Chapter 24, p921-22 2.2 DNA replication, semi-conservative replication, origin of replication, replication fork Chapter 25, p950-52 2.3 Leading and lagging strand synthesis, okazaki fragment Chapter 25, p952 2.4 Functions of proteins and enzymes required for DNA replication Chapter 25, p952-63 2.5 Mutation and repair mechanism Chapter 25, 966-78 Leading questions: - What is the semi-conservative DNA replication? - How can replication of mammalian DNA which is much bigger than the prokaryotic DNA being carried out in just a few minutes? - What are the functions of topoisomerase, helicase, single stranded binding protein, primase, DNA polymerase and DNA ligase? - What are the functions of DNA polymerase I and III? - Why DNA replication is so accurate? Learning Organization: 1. Lecture 100 min. 2. Q&A 10 min.
  41. 41. 41 3. Study from the course textbook Learning Materials provided: • List of suggested readings. Student Assessment: Multiple-choice questions with short (written) explanations.
  42. 42. 42 LESSON PLAN Lecture 18: DNA Replication Repair and Recombination Instructor: Sarawut, Biochemistry, Faculty of Science, Date/time: Wednesday, 25 January 2013, 13:30-16:20 Room: OP- Learning objectives: Students should be able to RNA metabolism 1. list components required for transcription 2. explain the component and function of RNA polymerase 3. explain the function of promoter 4. describe steps of transcription 5. describe posttranscriptional modification of RNAs Protein synthesis 1. explain the terms “codon”, anticodon”, wobble base and meaning of genetic code 2. discuss the factors require for translation 3. explain steps of translation 4. explain how the peptide bonds are form between amino acids during translation 5. explain the actions of some antibiotics on protein synthesis 6. discuss how nuclear encoded proteins are transported to organelles Content Outlines: RNA metabolism 1. Transcription (initiation, elongation and termination) Chapter 26, p996-1003 2. functions of various proteins and enzymes required for transcription Chapter 26, p996- 1003 3. Promoter recognition and RNA polymerase Chapter 26, p999,1003 4. RNA processing:mRNA, rRNA and tRNA Chapter 26, p1007-17 5. Reverse transcriptase Chapter 26, p1021-24 Leading questions: - What determine the boundary of gene? - What is the function of TATA-box? - What are the functions of sigma factor and core RNA polymerase? - What is the importance of 5‟-capping, intron removal and 3‟-polyadenylation? - Why can some single-copied genes produce multiple isoforms of encoded proteins? Protein synthesis 1 Genetic code, triplet codon, open reading frame Chapter 27, p1034-44 2. Ribosome structure and component Chapter 27, p1045-48 3. tRNA Chapter 27, p1049-55 4. Translation initiation, elongation and termination Chapter 27, p1056-62 5. Effect of antibiotics on protein synthesis Chapter 27, p1065-67 6. Protein targeting Chapter 27, p1068-73 Leading questions: - What is the meaning of non-overlapping triplet codon? - How is mRNA stabilized on the ribosome? - What is a maximum number of genetic codes that are recognized by tRNA?
  43. 43. 43 - How does tRNAs carry amino acids? - What is the function of peptidyl transferase? - Why does protein synthesis consume high energy? - How are many proteins imported to plasma membrane, mitochondria and nucleus? - Why do some antibiotics affect protein synthesis of prokaryote but not eukaryote Learning Organization: 1. Lecture 160 min. 2. Q&A 10 min. 3. Study from the course textbook Learning Materials provided: • List of suggested readings. Student Assessment: Multiple-choice questions with short (written) explanations.
  44. 44. 44 LESSON PLAN Lecture 19: Gene Expression and Regulation Instructor:: Sumalee, Biochemistry, Faculty of Science Date/Time: Friday, 28 January, 2013, 8:30-10:20 Room: OP- Learning Objective: Students are expected to accomplishing the following tasks: 1. Describe the molecular basis of transcription and translation control. 2. Apply knowledge to explain normal developmental physiology and pathogenesis. Content Outline: 1. Classification and basis of transcription control. 1.1 Gene organization and control. 1.2 Transcription control in virus and bacteria. 2. Eukaryotic transcription control. 2.1 Components and complexity of transcription control in eukaryotes. 2.2 RNA processing. 2.3 DNA and histone modifications. 2.4 The role of non-coding RNAs in gene regulation. 3. Classification and basis of translation control. 3.1 Control of translation machinery assembly. 3.2 Diseases caused by translation defects. Learning Organization: 1. Lecture presentation. 2. Questions and answers. Reading Material: 1. Class handout. 2. Lehninger Principles of Biochemistry 5th edition, 2009. Leading questions: Principles of gene regulation • What are the different levels of gene regulation in living cells and what are their roles ? (P. 1081) • What is the advantage of regulating gene expression at the transcriptional level ? (P. 1082) • What are „constitutive‟ and „regulated‟ gene expression ? How different are their roles ? (P. 1082) • What are „induction‟ and „repression‟ of gene expression ? (P. 1082) • What are the roles of transcription factors ? How many different types are there ? How do they work to regulate transcription ? (P. 1082-1083) • What are „positive‟ and „negative‟ regulations ? How are they different ? How do they regulate gene expression ? (P. 1084) Prokaryotic gene expression • What is an „operon‟ ? What are the components of an operon, their function, and organization within the operon ? (P. 1085) • How is „Lac Operon‟ subjected to „negative regulation‟ by lactose ? What happens in the absence/presence of lactose ? (P. 1085-1087)
  45. 45. 45 • What are the „inducer‟ of Lac Operon ? What are the roles of lactose, allolactose and IPTG in regulating Lac Operon ? (P. 1087) • How is „Lac Operon‟ subjected to „positive regulation‟ by glucose ? What is „catabolite repression‟ ? (P. 1093-1094) • What happens when both lactose and glucose are present ? (P. 1093-1094) Eukaryotic gene expression • What makes gene regulation in prokaryote and eukaryote different ? (P. 1102) 57 • What are „heterochromatin‟ and „euchromatin‟ ? How do they regulate gene expression in eukaryote ? Do they have a role in regulating gene expression in prokaryote ? (P. 1102) • How does chromatin remodeling occur ? What is the role in regulating eukaryotic gene expression ? (P. 1103) • What is the meaning of „positive regulation‟ ? (P. 1103) • Why are most eukaryotic genes under „positive‟ regulation ? (P. 1104) • How are eukaryotic genes regulated by intercellular signals such as steroid hormones ? (P. 1108) Student Assessment: MCQ or written exam.
  46. 46. 46 LESSON PLAN Lecture 20: DNA Technology Instructor: Sumalee, Biochemistry, Faculty of Science Date/Time: Wednesday, 30 January 2013, 10:30–12:20 Room: OP- Learning Objectives: Students are able to 1. define the techniques of gene cloning and the methods of creating restriction maps 2. recite polymerase chain reactions, DNA or genome sequencing, gene expressions and proteomes 3. look at the practical benefits and human issues of genetic engineering Content Outlines: 1. DNA cloning: The basics (Chapter 9) Leading Questions: - What is DNA cloning or definition of DNA cloning? (pp.306-307) - What is the function of restriction enzyme? What is the structure of palindromic sequence? (pp.308-309) - How many types of cloning vectors? (pp. 311-315) - How difference between gDNA library and cDNA library? (pp.318-319) 2. Polymerase chain reactions (Chapter 9) Leading Questions: - What is the key step of PCR? (pp.319-321) - What is a definition of primer? (pp.319-321) 3. DNA or genome sequencing (Chapter 8 and 9) Leading Questions: - How many methods to determine DNA sequences? (pp. 296-299) - Which strategy use to study DNA or genome sequences? (pp. 321-322) 4. Gene expression and proteomes (Chapter 9) Leading Questions: - How can we know the protein function? (pp.325) - Which methods do we use to study proteomes? (pp.326) - What are DNA microarrays and protein chips? (pp. 326-328) 5. Genome alterations and new products of Biotechnology and Medicine (Chapter 9) Leading Question: - Give an example on DNA technology yields new products and challenges? (pp.336-338) Learning Organization: 1. Lecture 100 min. 2. Q&A 10 min. 3. Study from the course textbook Reference: Lehninger Principles of Biochemistry by Nelson and Cox, 4th Edition, 2005 Student Assessment: Multiple-choice questions with short (written) explanations.
  47. 47. 47 LESSON PLAN Laboratory 4: DNA Isolation, PCR and Gel electrophoresis Lab Coordinator: Sumalee, Biochemistry, Faculty of Science Date/Time: Friday, 1 February 2013, 13:30–16:20 Room: OP- , MDL SC3-304, 308, 404, 408 Learning Objectives: Students should be able to 1. Isolate genomic DNA from white blood cells 2. Know basic technique to amplify target DNA by Polymerase chain reaction (PCR) 3. Describe the relationship among MW of biomolecules, type of supporters and electrical field 4. Visualize migrated DNA in an agarose gel electrophoresis 5. Determine MW or size in basepair or shape of DNA molecules Content Outlines: 1. Principle and how to isolate genomic DNA from algal cells 2. Principle and how to do the PCR reaction. 3. Principle and how to use electrophoresis technique 4. Determination of DNA molecules both in qualitative and quantitative analysis Learning Organization: 1. Studying the laboratory manual provided in advance. 2. Lab preview 30 min, Room L04. 3. Pre-test or homework to prepare a flow chart. 4. Hand on laboratory experiment. 5. Laboratory discussion Learning Materials Provided: 1. Laboratory manual 2. Chemicals, equipments for laboratory test. References: 1. Laboratory manual 2. Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 2nd edition, Worth, New York, 1993. 3. Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990. Student Assessment: For processes evaluation: 5% per lab • Quiz or pre-test and Attendance 30% • Report (by Group) 40% • Post test (Lab discussion) 30%
  48. 48. 48 LESSON PLAN Small Group Conference 3: Molecular Technology in Medicine Conference Coordinator: Sumalee, Biochemistry, Faculty of Science Date/Time: Monday, 4 February 2013, 8:30-10:20 Room: SC1-4 Learning Objectives: Students should be able to 1. apply knowledge from class to study principles of new technology. 2. discuss how DNA technology can be used to improve diagnostic and therapeutic platforms. Conference Outlines: 1. Molecular mechanisms underlying PCR and hybridization. 2. High-throughput DNA sequencing. 3. Personalized genome/Individualized Medicine. 4. Genetic engineering. Conference Questions: 1. What will happen to PCR reactions when you add too much DNA template (1010 fold)? Hint: consider DNA melting and annealing kinetics. 2. Explain the molecular process underlying pyrosequencing. What is its role in personalized genome? 3. Compare and contrast the Cambridge moratorium in the 1970s and the ongoing GMO controversy. Learning Organization: 1. Study from lecture materials, Lehninger, and extra reading materials. 2. Students are separated into three groups in advance to work on class presentations (one question per group). Class presentation 20 min. per group). 3. Questions and answers. And Quiz. Reading Materials: 1. Lehninger Principles of Biochemistry (4th edition) 2. http://www.pyrosequencing.com/DynPage.aspx?id=7454 3. Culliton BJ (1976) Recombinant DNA: Cambridge City Council votes moratorium. Science 193(4250):300-1. Student Assessment: 1. Students will be evaluated based on their presentations. 2. Post-test exam.
  49. 49. 49 LESSON PLAN CAI: Molecular Diagnostic, PCR and DNA Sequencing Coordinator: Sumalee, Biochemistry, Faculty of Science Date /Time: Wednesday, 6 February 2013, 10:30-12:20 Room: OP- Learning Objectives: Students will be able to 1. describe PCR, DNA sequencing and southern blotting processes and explain the molecular basis of these processes 2. describe DNA fingerprint and its applications CAI Outlines: 1. PCR 2. DNA sequencing 3. Southern blotting 4. DNA fingerprinting Learning Organization: 1. Study the learning materials (animation and VDO) in advance 2. Discussion with the group and hand in questions or points to discuss 24 hour before class. 3. In class, discussion and answering questions 50 min Learning Materials: 1. CAI programs installed in computers in MDL 2 and 3 2. Suggested websites References: • CD The Cell (Cooper), Molecular Cell Biology (Lodish) or Lehninger • Website: www.dnalc.org/resources/BiologyAnimationLibrary.htm Student Assessment: • Students will be asked by tutoring team members to perform some tasks or answer questions related to the CAI practice session. • Pre- or Post-test during all processes of learning
  50. 50. 50 LESSON PLAN Lecture 21: Biochemistry knowledge and medicine Instructor: Jamorn, Biochemistry, Faculty of Science Date/Time: Friday, 8 February 2013, 13.30-16.20 Room: OP- Learning Objectives Students will be able to 1. Describe some basic biochemistry knowledge in medical applications 2. Understanding of some changing in biochemistry parameters with disease status Content Outline 1. Explanation of basic blood biochemistry values 2. Effect of some physiological changes to biochemical compound in the body 3. Some diseases with some specific biochemical features 4. Some nutrition imbalances and pathogenesis via abnormal biochemistry 5. Enzyme kinetic with therapeutic applications 6. Some applications of DNA technology Learning Organization Studying the learning materials provided in advance 1. Lecture 100 min 2. Questions and answers 20 min Learning Materials Provided 1. Slides from PowerPoint lecture presentation References 1. Nelson, D. L., and Cox, M. M., Lehninger Principles of Biochemistry, 4th edition, W. H. Freeman and Company, New York, 2005 or comparable chapters in other text books. Student Assessment MCQ Exam
  51. 51. 51 LESSON PLAN TBL 1: Metabolic Syndrome TBL Staffs: Apirom and Team, Pathology, Faculty of Medicine Ramathibodi Hospital Date/Time: Monday, 12 March 2012, 8:30-10:20 Room: OP- Learning Objectives: Students are able to • Describe definitions of metabolic syndrome out of other metabolic diseases • Identify differences of fatty liver disease from alcoholic and non-alcoholic causes • Notice abnormal blood parameters which come from metabolic syndrome Suggested Reading Topics: • Goldman, L. and Schafer, A. Alcoholic and Nonalcoholic Steatohepatitis. Goldman‟s Cecil Medicine 24th Edition 996-999 References: Learning Organization: 1. Students study the learning materials given in advance according to the outlined content 2. Students will be tested individually for basic understanding in the TBL process 3. Students will be tested groups to clarify more understanding in the TBL process 4. Students will be challenged in groups to extend knowledge from their understanding in the TBL process Learning Materials provided: • Reading material provided in advance. • Problem sets and tests. Student Assessment: 1. Students will be evaluated by individual test and team members based test 2. Active participation
  52. 52. 52 LESSON PLAN Tutorial 2: Metabolic Integration and Nutrition Tutorial Staffs: Jamorn, Tuangporn, Wilai, Biochemistry, Faculty of Science Date/Time: Wednesday, 14 March 2012, 8:30-10:20 Room: OP- Learning Objectives: Students should be able to 1. raise questions regarding the lecture topics not understood to tutorial instructors. 2. spend the time in the tutorial to clarify lecture contents on metabolic pathways. Learning organization: 1. Students study the learning materials in advance according to the outline content and questions for students to answer after they study the content. 2. Students post any questions regarding the tutorial content prior to or at the tutorial session. 3. Questions are answered and explained at the tutorial session.
  53. 53. 53 LESSON PLAN Tutorial 3: Genetics and DNA Technology Tutorial Staffs: Sarawut, Sumalee, Biochemistry, Faculty of Science Date/Time: Friday, 16 March 2012, 13:30-16:20 Room: OP- Learning Objectives: Students should be able to 1. raise questions regarding the lecture topics not understood to tutorial instructors. 2. spend the time in the tutorial to clarify lecture contents on molecular genetics and DNA technologies. Learning organization: 1. Students study the learning materials in advance according to the outline content and questions for students to answer after they study the content. 2. Students post any questions regarding the tutorial content prior to or at the tutorial session. 3. Questions are answered and explained at the tutorial session.
  54. 54. 54 LESSON PLAN Tutorial 4: Xenobiotic and Drug Metabolism Tutorial Staffs: Krongtong, Somchai, Pharmacology, Faculty of Science Date/Time: Monday, 14 February 2011, 9:40-11:30 Room: OP- Learning Objectives: Students should be able to 1. raise questions regarding the lecture topics not understood to tutorial instructors. 2. spend the time in the tutorial to clarify lecture contents Learning organization: 1. Students study the learning materials in advance according to the outline content and questions for students to answer after they study the content. 2. Students post any questions regarding the tutorial content prior to or at the tutorial session. 3. Questions are answered and explained at the tutorial session.
  55. 55. 55 Small Group Conferences small group conferences PBL PBL 7 - Conference Group PBL Group Number 1 1 & 2 2 3 & 4 3 5 & 6 4 7 & 8 5 9 & 10 6 11 & 12 7 13 & 14 8 15 & 16 9 17 & 18 10 19 & 20 11 21 & 22 12 23 & 24 13 25 & 26 14 27 & 28 / Small Group Conference Conference Group Room Conference 1 Hemoglobin Structure and Function Friday, 14 December 2012, 13:30-16:20 Conference 2 Active Leaning Lesson: Diabetes Monday 7 January 2013, 8:30-10:20 Conference 3 Molecular Technology in Medicine Monday 4 February 2013, 8:30-10:20 1 SC1-139 (BC) (BC) (BC) 2 SC1-141 (BC) (BC) (BC) 3 SC1-220 (BC) (BC) (BC) 4 SC1-221 (BC) (BC) (BC) 5 SC1-321 (BC) (BC) (BC) 6 SC1-322 (BC) (BC) (BC) 7 SC2-133 (BC) (BC) (BC) 8 SC2-134 (BC) (BC) (BC) 9 SC2-136 (BC) (BC) (BC) 10 SC2-139 (BC) (BC) (BC) 11 SC2-140 (BC) (BC) (BC) 12 SC2-142 (PS) (RA) (IMB) 13 SC2-222 (IMB) (PS) (IMB) 14 SC2-322 (IMB) (IL) (IMB)
  56. 56. 56 PBL Hunger Strike Meeting 1 Section I 30 November 2012, 13:30-16:20 Section II 3 December 2012, 8:30-10:20 (BC) SC1-139 (BC) SC1-139 (BC) SC1-141 (BC) SC1-141 (BC) SC1-220 (BC) SC1-220 (BC) SC1-221 (BC) SC1-221 (BC) SC1-321 (BC) SC1-321 (BC) SC1-322 (BC) SC1-322 (RA) SC2-133 (RA) SC2-133 (PS) SC2-134 (PS) SC2-134 (PM) SC2-136 (PM) SC2-136 (PM) SC2-139 (PM) SC2-139 (PM) SC2-140 (PA) SC2-140 (PS) SC2-142 (PS) SC2-142 (AN) SC2-222 (BC) SC2-222 (RA) SC2-322 (RA) SC2-322 Meeting 2 Section I 11 January 2013, 13:30-16:20 Section II 14 January 2013, 8:30-10:20 (BC) SC1-139 (BC) SC1-139 (BC) SC1-141 (BC) SC1-141 (BC) SC1-220 (BC) SC1-220 (BC) SC1-221 (BC) SC1-221 (BC) SC1-321 (BC) SC1-321 (BC) SC1-322 (BC) SC1-322 (RA) SC2-133 (RA) SC2-133 (PS) SC2-134 (PS) SC2-134 (PM) SC2-136 (PM) SC2-136 (PM)) SC2-139 (PM) SC2-139 (PM) SC2-140 (PM) SC2-140 (BC) SC2-142 (PS) SC2-142 (AN) SC2-222 (BC) SC2-222 (RA) SC2-322 (RA) SC2-322
  57. 57. 57 57 PBL 1 5 Group :I PI-PBL 1-8, BM PBL 9-14, Group II RA PBL 15-28 PBL 1 1 5522003 2 5522006 3 5522017 3 5522022 5 5522038 6 5522055 7 5522061 8 5522070 9 5522079 10 5522096 11 5522103 11 5522107 12 5522115 14 5522131 PBL 2 1 5522004 2 5522007 3 5522019 4 5522037 5 5522040 6 5522056 7 5522062 8 5522074 9 5522080 10 5522098 * 11 5522105 12 5522116 13 5522122 14 5522132
  58. 58. 58 58 PBL 3 1 5522005 2 5522012 4 5522033 4 5522039 5 5522043 * 6 5522057 7 5522068 8 5522075 * 9 5522081 10 5522099 12 5522118 13 5522121 * 13 5522133 14 5522134 PBL 4 1 5522008 2 5522015 3 5522028 4 5522041 5 5522047 * 6 5522059 7 5522069 8 5522082 9 5522085 10 5522100 11 5522108 12 5522123 13 5522136 14 5522139
  59. 59. 59 59 PBL 5 1 5522009 2 5522021 3 5522029 4 5522042 5 5522048 6 5522060 7 5522071 8 5522084 9 5522086 10 5522106 * 11 5522111 12 5522124 13 5522137 14 5522140 PBL 6 1 5522010 2 5522025 3 5522030 4 5522044 5 5522050 6 5522063 7 5522072 8 5522088 9 5522089 10 5522109 11 5522114 12 5522128 13 5522138 14 5522141 15 5422077
  60. 60. 60 60 PBL 7 1 5522011 2 5522027 3 5522031 4 5522045 5 5522052 6 5522066 7 5522073 8 5522090 9 5522091 10 5522112 11 5522119 12 5522129 13 5522142 14 5522143 PBL 8 1 5522013 2 5522032 * 3 5522034 4 5522053 5 5522054 6 5522067 7 5522078 8 5522093 9 5522097 10 5522113 11 5522120 12 5522130 13 5522144 14 5422114
  61. 61. 61 61 PBL 9 1 5514001 2 5514007 3 5514014 4 5514020 5 5514026 6 5514032 7 5514038 8 5514041 9 5514047 10 5514054 11 5514060 12 5514066 13 5514072 PBL 10 1 5514002 2 5514008 3 5514015 4 5514021 5 5514027 6 5514033 7 5514042 8 5514048 9 5514055 10 5514061 11 5514067 12 5514073 13 5514078
  62. 62. 62 62 PBL 11 1 5514003 2 5514009 3 5514016 4 5514022 5 5514028 6 5514034 7 5514039 8 5514043 9 5514049 10 5514056 11 5514062 12 5514068 13 5514074 PBL 12 1 5514004 2 5514011 3 5514017 4 5514023 5 5514029 6 5514035 7 5514044 8 5514050 9 5514057 10 5514063 11 5514069 12 5514075 13 5514079
  63. 63. 63 63 PBL 13 1 5514005 2 5514012 3 5514018 4 5514024 5 5514030 6 5514036 7 5514040 8 5514045 9 5514051 10 5514058 11 5514064 12 5514070 13 5514076 PBL 14 1 5514006 2 5514013 3 5514019 4 5514025 5 5514031 6 5514037 7 5514046 8 5514053 9 5514059 10 5514065 11 5514071 12 5514077 13 5514080
  64. 64. 64 64 PBL 15 1 5502001 2 5502004 3 5502018 4 5502042 5 5502044 6 5502067 7 5502081 8 5502088 9 5502112 10 5502122 11 5502134 12 5502149 13 5502165 PBL 16 1 5502002 2 5502012 3 5502019 4 5502045 5 5502046 6 5502068 7 5502086 8 5502091 9 5502113 10 5502125 11 5502135 12 5502151 13 5502167
  65. 65. 65 65 PBL 17 1 5502003 2 5502016 3 5502021 4 5502047 5 5502048 6 5502070 7 5502089 8 5502094 9 5502114 10 5502126 11 5502138 12 5502152 13 5502169 PBL 18 1 5502005 2 5502020 3 5502022 4 5502049 5 5502050 6 5502073 7 5502090 8 5502095 9 5502116 10 5502129 11 5502140 12 5502154 13 5502170
  66. 66. 66 66 PBL 19 1 5502006 2 5502023 3 5502025 4 5502051 5 5502055 6 5502074 7 5502092 8 5502096 9 5502117 10 5502131 11 5502141 12 5502155 13 5502171 PBL 20 1 5502007 2 5502024 3 5502028 4 5502052 5 5502056 6 5502075 7 5502093 8 5502097 9 5502119 10 5502133 11 5502146 12 5502156 13 5502172
  67. 67. 67 67 PBL 21 1 5502008 2 5502026 3 5502030 4 5502053 5 5502057 6 5502076 7 5502098 8 5502101 9 5502120 10 5502136 11 5502147 12 5502174 PBL 22 1 5502009 2 5502027 3 5502031 4 5502054 5 5502058 6 5502077 7 5502099 8 5502103 9 5502121 10 5502137 11 5502150 12 5502157 13 5502175
  68. 68. 68 68 PBL 23 1 5502010 2 5502029 3 5502032 4 5502059 5 5502064 6 5502079 7 5502100 8 5502104 9 5502123 10 5502139 11 5502153 12 5502160 PBL 24 1 5502011 2 5502033 3 5502034 4 5502060 5 5502069 6 5502082 7 5502102 8 5502105 9 5502124 10 5502142 11 5502158 12 5502162 13 5502176
  69. 69. 69 69 PBL 25 1 5502013 2 5502035 3 5502037 4 5502062 5 5502071 6 5502083 7 5502106 8 5502107 9 5502127 10 5502143 11 5502159 12 5502166 PBL 26 1 5502014 2 5502036 3 5502038 4 5502063 5 5502072 6 5502084 7 5502108 8 5502111 9 5502128 10 5502144 11 5502161 12 5502168 13 5502178 --------------------------
  70. 70. 70 70 PBL 27 1 5502015 2 5502039 3 5502041 4 5502065 5 5502078 6 5502085 7 5502109 8 5502115 9 5502130 10 5502145 11 5502163 12 5502173 PBL 28 1 5502017 2 5502040 3 5502043 4 5502066 5 5502080 6 5502087 7 5502110 8 5502118 9 5502132 10 5502148 11 5502164 12 5502177 13 5502179 --
  71. 71. 71 71 SCID 5 6 --

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