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    CHEM 4500 new.doc CHEM 4500 new.doc Document Transcript

    • KENNESAW STATE UNIVERSITY UNDERGRADUATE PROPOSAL New Course (NOT General Education) I. Proposed Information Course Prefix and Number: ___CHEM 4500_________________ Course Title: _______ Methods in Nucleic Acid and Protein Biochemistry ______________ Credit Hours (format should be # - # - #): ___2-3-3_________ Prerequisites: _____CHEM 3501 and 3501L and BIOL 3300_____________________________ (Prerequisites are courses or requirements that non-negotiable and must be successfully completed by any student before enrolling in the course or program under consideration. Corequisites are courses that can be taken before or in the same semester as the course under consideration. Courses at the upper-division level will require lower-division competencies or prerequisites.) Course Description for the Catalog: This course covers the chemical aspects of biochemical techniques routinely performed in the study of DNA, RNA, and protein. This course will build upon and complement the information on proteins and enzymes covered in biochemistry courses and the basic understanding of DNA, RNA, replication, transcription, and translation that students learn in biochemistry, genetics and other biology courses. The laboratory component of this course provides an opportunity for multi-week projects that combine methods learned in previous courses with new methods, and as such it serves as a capstone experience in biochemical methodology. II. Justification for Course A. Explain assessment findings which led to course development. Previously some of this content was covered in the BTEC 4100 course and this course was listed as a requirement for the B.S. Biochemistry degree. In Fall 2005, due to an increased number of biochemistry majors, an additional section of BTEC 4100 was needed to accommodate the senior level B.S. Biochemistry majors. In providing a temporary solution by offering CHEM 4510 (Advanced Topics in Biochemistry) and allowing students to substitute this course for BTEC 4100, we examined in detail the material covered in BTEC 4100 and re-evaluated the information we felt a biochemistry major should receive. We determined that while the existing BTEC 4100 course covered DNA topics extensively, our majors also needed molecular methods coverage of protein and RNA. In addition, we felt that biochemistry majors needed to understand the chemistry that was occurring in the biological methods they were using and how to design changes in DNA that would result in desired changes in protein structure. Our plan is to have this new course, CHEM 4500 replace the requirement of BTEC 4100 for the B.S. Biochemistry program. B. Explain for Prerequisites: 1. What is the substance of content in each prerequisite that commands its inclusion as a prerequisite to the proposed course? The techniques require knowledge of the structure of DNA
    • and replication and transcription which are covered in BIOL 3300 and CHEM 3501. It also requires knowledge of enzymes and other proteins which are covered in CHEM 3501 and lab skills which are gained in CHEM 3501L. 2. What is the desired sequence of prerequisites? Both must be taken before CHEM 4500; however, the order does not matter. 3. What is the rationale for requiring the above sequence of prerequisites? N/A 4. How often are the required prerequisites offered? CHEM 3501/L and BIOL 3300 are offered in both fall and spring. BIOL 3300 is also sometimes offered in summer. B. Give any other justification for the course. Students in Biochemistry I lab learn how to work with both proteins and DNA on an introductory level. These experiments are simple manipulations that consist of individual one lab session experiments. A working biochemist or a graduate student in biochemistry needs to understand how these techniques fit together in a unified project. Biochemistry majors are already required to take an advanced biochemistry lab course or 2 credits of directed study (independent research project). This lab focuses on protein expression and purification, separation of small biological molecules, and immunoassays (techniques that use antibodies as part of the detection). However, these requirements alone do not expose the students to DNA or RNA to any significant extent. Today’s biochemist needs to be able to work with DNA and RNA in cells in order to produce proteins for study. This may include normal proteins or mutant proteins (modified versions of the normal protein). The existing BTEC 4100 DNA methods course is limited to DNA technologies. We are proposing this course as a capstone course that will connect what the students learn about DNA and RNA in genetics (BIOL 3300) and what they know of proteins (from CHEM 3501) and build on lab techniques learned in CHEM 3501L. They will learn how to manipulate DNA emphasizing the enzymes used, how to amplify DNA, and the techniques used to transfer DNA into bacterial, mammalian, or yeast cells for the purpose of protein production. They will be introduced to handling RNA since it varies from that of DNA. Finally students need to be exposed to current biochemistry methods to study protein-DNA interaction since the field changes so quickly with the development of new techniques. Since the course will be taught with a combined lecture-laboratory approach the students will be able to study the techniques both theoretically and practically, while the long-term project aspect will allow the students to appropriately modify and troubleshoot the most common biochemical procedures. III. Additional Information A. Where does this course fit sequentially and philosophically within the program of study? The course would be taken in the last year of study as a capstone experience. This timing is required since a year of general chemistry, a year of organic chemistry, and at least one semester of biochemistry must be taken prior to this course. B. What efforts have been made to ensure that this course does not duplicate the content of other college courses with similar titles, purposes, or content? BTEC 4100 is the only other course that is similar to the course being proposed, however, as stated in the assessment, that course only covers DNA, while this course covers DNA, RNA, and protein. Repetitiveness is also limited due to the use of DNA techniques with a focus of using DNA as a tool to study proteins, rather than for the study of DNA itself (as BTEC 4100 does). Also, we are making this a capstone course which will require students to draw upon content from CHEM 3501/L and BIOL 3300 which makes it very different from BTEC 4100.
    • C. Where will the course be located in the program (elective, required in Area F, required or elective for the major)? Indicate and justify its placement in the curriculum. The course will be required for the B.S. Biochemistry degree, and be an elective for other majors. This requirement is justified due to the role that molecular biology plays in current biochemical techniques. D. How often will this course be offered? The course will initially be offered once a year in the fall semester and more frequently as dictated by enrollment. E. All sections of the course will be taught with the understanding that the following apply: 1. Purpose of the Course: To provide a capstone experience that allows students to integrate previous knowledge with new material for long term projects and allows students to connect ideas learned in different courses (biochemistry, biochemistry lab, genetics) in a more cohesive manner. Since the course will be taught with a combined lecture-laboratory approach the students will be able to study the techniques both theoretically and practically, while the long-term project aspect will allow the students to appropriately modify and troubleshoot the most common biochemical procedures. 2. Objectives of the Course: Students will learn to develop unique protocols, to firmly grasp basic molecular techniques, to be introduced to ways to find troubleshooting information on their own for future use in laboratory settings and they will be exposed to cutting edge molecular techniques used in the field of biochemistry. 3. Course Content: Basic review of DNA transcription and translation. Complete coverage of the basic molecular techniques including, but not limited to, detection methods, PCR, and mammalian tissue culture. DNA manipulation emphasizing the enzymes used, how to amplify DNA, and the techniques used to transfer DNA into bacterial, mammalian, or yeast cells for the purpose of protein production. How working with RNA varies from working with DNA. Current biochemistry methods to study protein-DNA interactions. The remainder of the course will vary from year to year as new methodologies become available and as equipment and faculty expertise allows. F. What instructional methodologies will be incorporated into the course to stimulate group process, writing skills, multiculturalism, and educational outcomes? Group process is incorporated through unique assignments that overlap in basic concepts so that students can work together to design projects and discuss project troubleshooting strategies, while still being responsible for their own unique project end point. Since the class as a whole will share reagents that individuals prepare, the group experience will also emphasize the importance of being able to trust others work when performing as a group. Since the project methodologies and results must be written, this further enhances scientific writing methods. The predominant educational outcome is to enhance the students’ ability to take pieces of information and weave them into a large project. G. Outline the plan for continuous course assessment. What are the department, school, college, or professional standards which will be used for the assessment? How will it be determined that the course is current, meeting the educational needs of students and responsive to educational standards? How often will the course assessment be done by the department? The course will be assessed by the faculty on an annual or biannual basis to ensure that new methodologies are incorporated. Cold Spring Harbor Laboratories in New York is one of the leaders in molecular techniques. They publish a Molecular Cloning laboratory manual that is updated several times
    • a year to stay abreast of the most recent technologies. The course will be checked against the contents of this lab manual for any new material in the field of molecular biochemistry. On a departmental level, this course will be added to the current Assurance of Learning (AOL) document that the Chemistry department is developing, and as such join the rotation of curriculum assessment. The specific AOL learning outcomes for this course are listed on the syllabus. H. Enclose a course syllabus (optional format described at the end of this document) See attachment. IV. Resources and Funding Required A. What resources will be redirected to accommodate this course? None B. Explain what items will cause additional cost to the department/school/college Personnel: None Computer Technology: All relevant software can be obtained with a free educational license the semester that the course is taught. Library resources: None Equipment: None Space: None
    • SAMPLE SYLLABUS CHEM 4500: Methods in Nucleic Acid and Protein Biochemistry Instructor: Dr. Carol Chrestensen Office: SC422 Phone: 770-499-3525 Email: cchreste@kennesaw.edu Textbook: Lewin, Benjamin, Genes VIII , Copyright 2004, Pearson Prentice Hall, NJ Supplemental Texts: Horton, et al. Principles of Biochemistry, 3rd Ed. Brooker. Genetics: Analysis and Principles, 2nd Ed. Molecular Cloning, 3rd Ed. On-line: National Center for Biotechnology Information www.ncbi.nlm.nih.gov Invitrogen, iProtocol online library, VectorNTI www.invitrogen.com New England Biolabs, NEB Cutter, www.neb.com The ExPASy (Expert Protein Analysis System) proteomics server of the Swiss Institute of Bioinformatics (SIB) http://ca.expasy.org/ Pre-requisites: “C” or better grade in CHEM 3501 and 3501L and BIOL 3300 Learning Objectives: The purpose of this course is to integrate everything that you have learned in your courses and labs up to this point into understanding the complete laboratory skills that you will use as a Biochemist. The course will be technique based, and will build upon the DNA transcriptional and translational information that is learned in Genetics, as well as the structural information that you learned about biological molecules in Biochemistry. This course is expected to fulfill the Assurance of Learning Outcomes (from the Biochemistry AOL document). Main Learning Outcomes: 1. Discuss molecular structure of vectors and explain why vectors have been genetically engineered to be used as laboratory tools in cloning. 2. Read a plasmid map and obtain information necessary for inserting a particular gene in order for it to be expressed. 3. Know common enzymes and requirements for enzymatic reactions commonly used to manipulate DNA: restriction enzymes, ligases, and polymerases. 4. Summarize the uses of the polymerase chain reaction (PCR) and be able to perform PCR. 5. Identify key differences between lab protocols involving DNA and those involving RNA. 6. Distinguish between methods of introducing DNA into bacterial, mammalian, and yeast cells. 7. Relate DNA manipulations to expression of protein for biochemical studies. 8. Describe various methods of detecting protein-protein and protein-DNA interactions.
    • I. Critically select the best type of detection assay based on analysis of chemical properties, sensitivity limits, and safety factors. II. Design experimental procedures and be able to apply troubleshooting techniques when problems arise in published protocols. Tentative Course Schedule Class Topics Chapter(s) Lab Topics Projects Intro - Standards, variables, and Aug 22 constants Hypotheses - Finding protocols #1 DNA 24 DNA and Genes 1,2 Reagents/ Methods Unknowns 29 Genes 3, 4 Design 31 mRNA 5 Start DNA Unknowns Due Sept 5 Sept 5 mRNA and Transcription 5,9 Report 7 Vectors 13,14 Purification of DNA due Sept 12 Transformation 26 14 Restriction Digestion Vector NTI 19 Plasmids/ Ligation 21 Exam 1 Open Lab time 26 PCR 28 Real time PCR Open Lab time #2 Reverse transcriptase PCR/ Creating Oct 3 Mutagenesis Point 5 DNA sequencing Open lab time Mutations 10 Southern Blotting: Detection methods in DNA 12 Western & Northern Blotting Open lab time Design due 17 Mammalian tissue culture Oct. 3 19 Exam 2 Open Lab time Report due Nov 2 24 No Class Getting to know 26 Protein Expression Electrophoresis/Blotting equipment 31 Presentations #3 Protein Nov 2 Presentations Presentations –Protein or 7 Chromatography protein- 9 Transfection/SiRNA Open Lab time DNA interactions 14 DNA –protein interactions (EMSA) due Nov. 9 16 Protein-Protein interactions Open Lab time Report 21 Exam 3 due Dec. 5 23 No Class Open Lab time 28 Transgenic mice 30 Mass Spectrometry Open Lab time Dec 5 Final Exam Review 7 Final Exam - 2- 4 pm GRADING: 3 Tests (Drop lowest) 30% Lab Reports & Notebooks 30%
    • Presentation 20% Final Exam 15% Class Participation 5% Grading Scale: 90-100 A 80.89 B 70.79 C 60.69 D <60 F Class Attendance: Since many of the lectures are on current technology, there will often be class discussions. Each missed discussion will result in a loss of a half percent from the class participation grade. It is expected that everyone present will contribute at least once in every discussion. Failure to do so can cause the same loss of a half percent. Projects: There will be three projects. Everyone will complete all three projects and each project will be unique for each student, therefore you can discuss projects with other students. There are two parts to each project that will be graded. Part one is the design of the experiment. This design should include everything (buffers, standards, variables, constants, as well as potential pitfalls that you may encounter.) This portion is due Sept 27, Nov 1, and Nov 29. Part two is the actual completion of the project and presentation of this work in a Journal style lab report. These reports will be due in a timely fashion as we move into new projects but the final report will be due by the last lab session (Dec 5th at 5PM). Presentations: There will be one presentation, on a Journal article of your choosing that will be approved by the instructor. The presentation will be on a PCR based method, it will be 15 minutes in length but there will be an opportunity at the end for classmates and the instructor to ask questions. KSU Policies: Integrity: Every KSU student is responsible for upholding the provisions of the Student Code of Conduct, as published in the Undergraduate Catalog. Section II of the Student Code of Conduct addresses the University’s policy on academic honesty, including provisions regarding plagiarism and cheating, unauthorized access to University materials, misrepresentation / falsification of University records or academic work, malicious removal, retention, or destruction of library materials, malicious / intentional misuse of computer facilities and / or services, and misuse of student identification cards. Incidents of alleged academic misconduct will be handled through the established procedures of the University Judiciary Program, which may subject a student to the Code of Conduct’s minimum one semester suspension requirement. Suspicious behavior can get you in trouble. Keep your eyes on your own paper during Quizzes and Exams. Be careful to prevent other students from seeing your paper during Quizzes and Exams. Non-medical electronic devices may not be used during exams. Withdrawal: "W" grades on your transcript are a negative factor in evaluating your academic performance. For anyone serious about a professional or graduate school of any kind, I would recommend that your transcript should show no more than 4 "W" grades, and you should have an excellent reason for each one. I will help in any way
    • possible to avoid this situation; however it is always better to approach me (or a tutor) while you can still pull up your grade, do not wait until just before the final! As of Fall 2004, students will be allowed a maximum of eight total withdrawals if they enter KSU as a freshman. Transfer students will be allowed one withdrawal per fifteen credit hours attempted, for a maximum of eight. Students who choose to pursue a second degree at KSU will be allowed two additional withdrawals. Students who entered KSU before the fall of 2004 will be allowed one withdrawal per fifteen credit hours attempted for a maximum of eight. To completely or partially withdraw from classes at KSU, a student must withdraw online at http://www.kennesaw.edu, under Owl Express, Student Services. The date the withdrawal is submitted online will be considered the official KSU withdrawal date which will be used in the calculation of any tuition refund or refund to Federal student aid and/or HOPE scholarship programs. It is advisable to print the final page of the withdrawal for your records. Withdrawals submitted online prior to midnight on the last day to withdraw without academic penalty will receive a "W" grade. This does not affect the grade point average. Withdrawals after midnight will receive a “WF”, which will be counted as an "F" in calculation of their grade point average. Failure to complete the online withdrawal process will produce no withdrawal from classes. Those students who stop attending classes and notify no one are usually assigned failing grades which jeopardize their chances of future academic success. Call the Registrar's Office at 770-423-6200 during business hours if assistance is needed. The last day to withdraw without academic penalty is October 13. Failure to withdraw by the appropriate date will mean that the student has elected to receive the final grades earned in the course. The only exceptions to these withdrawal regulations will be for those instances which involve unusual and fully documented circumstances. Disruption of Campus Life Statement: It is the purpose of the institution to provide a campus environment, which encourages academic accomplishment, personal growth, and a spirit of understanding and cooperation. An important part of maintaining such an environment is the commitment to protect the health and safety of every member of the campus community. Belligerent, abusive, profane, threatening and/or inappropriate behavior on the part of students is a violation of the Kennesaw State University Student Conduct Regulations. Students who are found guilty of such misconduct may be subject to immediate dismissal from the institution. In addition, these violations of state law may also be subject to criminal action beyond the University disciplinary process. Preview of Teaching Evaluation Questionnaire: The KSU faculty value student comments about the course, instructor and materials, etc., which can be used to improve teaching and learning. A survey consisting of the following questions will be distributed during the last two weeks of classes. Students should consider them during the term and be prepared to answer them. 1. Identify the aspects of the course that most contributed to your learning (include examples of specific materials, exercises and/or the faculty member’s approach to teaching, supervision and mentoring). 2. Identify the aspects of the course, if any,that might be improved (include examples of specific materials, exercises and/or the faculty member’s approach to teaching, supervision and mentoring).
    • V. COURSE MASTER FORM This form will be completed by the requesting department and will be sent to the Office of the Registrar once the course has been approved by the Office of the President. The form is required for all new courses. DISCIPLINE: ______Chemistry_________________________ COURSE NUMBER: _____CHEM 4500____________________ COURSE TITLE FOR LABEL: ___ Methods Nucleic Acid & Protein_____ (Note: Limit 30 spaces) CLASS-LAB-CREDIT HOURS: _____2-3-3___________ Approval, Effective Semester: ______Summer 2007____________ Grades Allowed (Regular or S/U): ____Regular____________ If course used to satisfy CPC, what areas? _______________________________________ Learning Support Programs courses which are required as prerequisites: ______None_____________________________________________ APPROVED: _______________________________________________________________________ Vice President for Academic Affairs or Designee
    • KENNESAW STATE UNIVERSITY UNDERGRADUATE PROPOSAL New Course (NOT General Education) Course Prefix and Number: ________CHEM 4500_______________________________ Responsible Department: _________Chemistry and Biochemistry___________________ Proposed Effective Date: _________Summer 2007________________________________ Signature Page Submitted by: __ ___________________________________________________ Name: Carol Chrestensen November 9, 2006 ___ Approved ___ Not Approved _____________________________ Department Curriculum Committee, Date ___ Approved ___ Not Approved _____________________________ General Education Council*, Date ___ Approved ___ Not Approved _____________________________ Professional Teacher Education Unit Program Area*, Date ___ Approved ___ Not Approved _____________________________ Department Chair, Date ___ Approved ___ Not Approved _____________________________ College/School Curriculum Committee AND/OR Teacher Education Council*, Date ___ Approved ___ Not Approved _____________________________ College/School Dean, Date ___ Approved ___ Not Approved _____________________________ Undergraduate Policies and Curriculum Committee, Date ___ Approved ___ Not Approved _____________________________ Dean of Undergraduate & University Studies, Date *For curriculum proposals involving General Education courses, there should be collaboration by the Department Curriculum Committee and the General Education Council. For Teacher Preparation proposals, there should be collaboration by the Department Curriculum Committee, the Professional Teacher Education Unit (PTEU) Program Area Committee, the Teacher Education Council, and the College/School Curriculum Committee. Form updated December 2, 2004.