Guided notes covering material from Topics 2.4 and 7.3 of the updated IB Biology syllabus for 2016 exams. Notes sequence and prompts are based on the Oxford IB Biology textbook by Allott and Mindorff.
Guided notes covering material from Topic 2.3 of the updated IB Biology syllabus for 2016 exams. Notes sequence and prompts are based on the Oxford IB Biology textbook by Allott and Mindorff.
Guided notes covering material from Topics 2.4 and 7.3 of the updated IB Biology syllabus for 2016 exams. Notes sequence and prompts are based on the Oxford IB Biology textbook by Allott and Mindorff.
Guided notes covering material from Topic 2.3 of the updated IB Biology syllabus for 2016 exams. Notes sequence and prompts are based on the Oxford IB Biology textbook by Allott and Mindorff.
Guided notes covering material from Topic 2.1 of the updated IB Biology syllabus for 2016 exams. Notes sequence and prompts are based on the Oxford IB Biology textbook by Allott and Mindorff.
This PPT is meant for undergraduate students to clear the concepts of Microbial metabolism.
The presentation includes the basics of catabolism and anabolism
Enzymes definitions, types & classificationJasmineJuliet
Enzyme - Introduction, Biocatalysts, Definition of enzymes, Types of enzymes, classification of enzyme, Nomenclature of enzymes, EC number, Types of enzymes with examples, and reaction.
Quantitative estimation of protein Likhith KLIKHITHK1
Proteins are polypeptide structures consisting of one or more long chains of amino acid residues. They carry out a wide variety of organism functions, including DNA replication, transporting molecules, catalyzing metabolic reactions, and providing structural support to cells. A protein can be identified based on each level of its structure. Every protein at least contains a primary, secondary, and tertiary structure. Only some proteins have a quaternary structure as well. The primary structure is comprised of a linear chain of amino acids. The secondary structure contains regions of amino acid chains that are stabilized by hydrogen bonds from the polypeptide backbone. These hydrogen bonds create alpha-helix and beta-pleated sheets of the secondary structure. The three-dimensional shape of a protein, its tertiary structure, is determined by the interactions of side chains from the polypeptide backbone. The quaternary structure also influences the three-dimensional shape of the protein and is formed through the side-chain interactions between two or more polypeptides. Each protein at least contains a primary, secondary, and tertiary structure. Only some proteins have a quaternary structure as well.
Accurate protein quantitation is essential to protein studies in a multitude of research topics. A wide array of different methods have been developed to quantitate both complex mixtures of proteins as well as a single type of protein.
Total protein quantitation methods comprise traditional methods such as the measurement of UV absorbance at 280 nm, Bicinchoninic acid (BCA) and Bradford assays, as well as alternative methods like Lowry or novel assays developed by commercial suppliers, which often provide a well-designed, convenient kit for each type of the assay. Individual protein quantitation methods include enzyme-linked immunosorbent assay (ELISA), western blot analysis, and more recently, mass spectrometry, among others. Accurate protein quantitation is essential to all experiments related to proteins studies in a multitude of research topics. Different wide array of different methods have been developed to quantitate both complex mixtures of proteins in a given assay for total protein content and as well as for a single type of protein.
The central dogma of molecular biology, the basic structure of nucleic acids, Genetic code, 4 levels of protein structure, Revision question with answers
Guided notes covering material from Topic 2.1 of the updated IB Biology syllabus for 2016 exams. Notes sequence and prompts are based on the Oxford IB Biology textbook by Allott and Mindorff.
This PPT is meant for undergraduate students to clear the concepts of Microbial metabolism.
The presentation includes the basics of catabolism and anabolism
Enzymes definitions, types & classificationJasmineJuliet
Enzyme - Introduction, Biocatalysts, Definition of enzymes, Types of enzymes, classification of enzyme, Nomenclature of enzymes, EC number, Types of enzymes with examples, and reaction.
Quantitative estimation of protein Likhith KLIKHITHK1
Proteins are polypeptide structures consisting of one or more long chains of amino acid residues. They carry out a wide variety of organism functions, including DNA replication, transporting molecules, catalyzing metabolic reactions, and providing structural support to cells. A protein can be identified based on each level of its structure. Every protein at least contains a primary, secondary, and tertiary structure. Only some proteins have a quaternary structure as well. The primary structure is comprised of a linear chain of amino acids. The secondary structure contains regions of amino acid chains that are stabilized by hydrogen bonds from the polypeptide backbone. These hydrogen bonds create alpha-helix and beta-pleated sheets of the secondary structure. The three-dimensional shape of a protein, its tertiary structure, is determined by the interactions of side chains from the polypeptide backbone. The quaternary structure also influences the three-dimensional shape of the protein and is formed through the side-chain interactions between two or more polypeptides. Each protein at least contains a primary, secondary, and tertiary structure. Only some proteins have a quaternary structure as well.
Accurate protein quantitation is essential to protein studies in a multitude of research topics. A wide array of different methods have been developed to quantitate both complex mixtures of proteins as well as a single type of protein.
Total protein quantitation methods comprise traditional methods such as the measurement of UV absorbance at 280 nm, Bicinchoninic acid (BCA) and Bradford assays, as well as alternative methods like Lowry or novel assays developed by commercial suppliers, which often provide a well-designed, convenient kit for each type of the assay. Individual protein quantitation methods include enzyme-linked immunosorbent assay (ELISA), western blot analysis, and more recently, mass spectrometry, among others. Accurate protein quantitation is essential to all experiments related to proteins studies in a multitude of research topics. Different wide array of different methods have been developed to quantitate both complex mixtures of proteins in a given assay for total protein content and as well as for a single type of protein.
The central dogma of molecular biology, the basic structure of nucleic acids, Genetic code, 4 levels of protein structure, Revision question with answers
In your own words discuss the following 1a. In what ways are macr.pdfpearlcoburnsanche303
In your own words discuss the following:
1a. In what ways are macromolecules essential to life?
1b. Describe the structures of four and describe their major roles in organisms?
2a. Briefly explain the overall processes of photosynthesis and cellular respiration?
2b. Also include a brief explanation of autotrophs and heterotrophs?
Solution
1a. Macromolecules are large molecules that serve as a source of energy, form the basic structure
of the organism and also carries the genetic information of the organism.
1b.proteins, carbohydrates, lipids and nucleic acids are the four macromolecules
proteins structure
primary
they are chains of aminoacids
secondary
these aminoacids can assume a folded confirmation to form a alpha helix or a beta pleated sheet
structure
this depepnds on the hydrogen bnding and electrostatic interactions between adjascent
aminoacids in the polymer
tirtiary
A protein on a whole can have many secondary structures which depends on the length of the
protein and also on the nature of aminoacids present in them.
For example when a protein has 2 alpha helix, the two helices are connected through disulfide
bridge or electrostatic force or even a small beta pleated sheet
this forms the secondary structure
Quarternary structure
to achieve the function of the proteins it has to be folded in the correct conformation which is
achieved in the quarternary structure.
Carbohydrate
it is basically a hydrocarbon
hydrogen bonding between sugar molecules will result in formation of a chain of sugar called
carbohydrates or polysaccharides
the sugars in the carbohydrate chain can be a simple carbon chain, a 5 carbon ring structure
(pentose) or a six carbon ring structure.
lipids:
they are also hydrocarbon chains however they will have a carboxyl group attached to the main
carbon.
nucleic acids:
they areof 2 forms DNA and RNA they have a sugar in the backbone
deoxyribose sugar in DNA and ribose sugar in RNA they have 4 bases that are bound to the
sugar backbone through phosphate bonding
DNA adenin,e guaninie, cytosine, thymine
RNA thymine replaced with Uracil
DNA double stranded with the two strands bound with hydrogen bonding between the bases A_T
and G_C
Proteins are essential as receptors in cells, structure on membrane, antigen on bacteria and is the
major body building macromolecule
Lipids are very rich source of energy so the body in general stores them for future use and uses
them under conditions of starving. lipids also have structural role.
Carbohydrates are major source of energy and are mostly metabolised to provide ATP for the
bodies function
2a. photosynnthesis is a process of fixing atmospheric CO2 into sugar molecule that is powered
by sunlight.
It uses CO2 and releases oxygen while respiration uses oxygen and releases CO2
Energy is utilised in the process of photosynthesis and the generated sugars are further broken
down to meet the energy needs of the organism.
2b autotrophs are those which can generate their own energy like plan.
Introduction about Biomolecules - I or Macromolecules introductionshoba shoba
Biomolecules are biological molecules produced by the cells of the living organism. They are critical for life as it helps organisms to carry out basic biological processes such as reproduction, growth and sustainence.
The Art Pastor's Guide to Sabbath | Steve ThomasonSteve Thomason
What is the purpose of the Sabbath Law in the Torah. It is interesting to compare how the context of the law shifts from Exodus to Deuteronomy. Who gets to rest, and why?
The Indian economy is classified into different sectors to simplify the analysis and understanding of economic activities. For Class 10, it's essential to grasp the sectors of the Indian economy, understand their characteristics, and recognize their importance. This guide will provide detailed notes on the Sectors of the Indian Economy Class 10, using specific long-tail keywords to enhance comprehension.
For more information, visit-www.vavaclasses.com
Instructions for Submissions thorugh G- Classroom.pptxJheel Barad
This presentation provides a briefing on how to upload submissions and documents in Google Classroom. It was prepared as part of an orientation for new Sainik School in-service teacher trainees. As a training officer, my goal is to ensure that you are comfortable and proficient with this essential tool for managing assignments and fostering student engagement.
Read| The latest issue of The Challenger is here! We are thrilled to announce that our school paper has qualified for the NATIONAL SCHOOLS PRESS CONFERENCE (NSPC) 2024. Thank you for your unwavering support and trust. Dive into the stories that made us stand out!
Model Attribute Check Company Auto PropertyCeline George
In Odoo, the multi-company feature allows you to manage multiple companies within a single Odoo database instance. Each company can have its own configurations while still sharing common resources such as products, customers, and suppliers.
Ethnobotany and Ethnopharmacology:
Ethnobotany in herbal drug evaluation,
Impact of Ethnobotany in traditional medicine,
New development in herbals,
Bio-prospecting tools for drug discovery,
Role of Ethnopharmacology in drug evaluation,
Reverse Pharmacology.
How to Make a Field invisible in Odoo 17Celine George
It is possible to hide or invisible some fields in odoo. Commonly using “invisible” attribute in the field definition to invisible the fields. This slide will show how to make a field invisible in odoo 17.
1. 2. Molecular Biology (Core) – 2.4 Proteins Name:
Understandings, Applications and Skills (This is what you maybe assessed on)
Statement Guidance
2.4.U1 Amino acids are linked together by condensation to form
http://bioknowledgy.weebly.com/ (Chris Paine)
polypeptides.
2.4.U2 There are 20 different amino acids in polypeptides
synthesized on ribosomes.
Students should know that most organisms
use the same 20 amino acids in the same
genetic code although there are some
exceptions. Specific examples could be
used for illustration.
2.4.U3 Amino acids can be linked together in any sequence giving
a huge range of possible polypeptides.
2.4.U4 The amino acid sequence of polypeptides is coded for by
genes.
2.4.U5 A protein may consist of a single polypeptide or more than
one polypeptide linked together.
2.4.U6 The amino acid sequence determines the three-dimensional
conformation of a protein.
2.4.U7 Living organisms synthesize many different proteins with a
wide range of functions.
2.4.U8 Every individual has a unique proteome.
2.4.A1 Rubisco, insulin, immunoglobulins, rhodopsin, collagen
and spider silk as examples of the range of protein
functions.
The detailed structure of the six proteins
selected to illustrate the functions of
proteins is not needed.
2.4.A2 Denaturation of proteins by heat or by deviation of pH from
the optimum.
Egg white or albumin solutions can be used
in denaturation experiments.
2.4.S1 Drawing molecular diagrams to show the formation of a
peptide bond.
Recommended resources:
http://bioknowledgy.weebly.com/24-proteins.html
Allott, Andrew. Biology: Course Companion. S.l.: Oxford UP, 2014. Print.
2. 2. Molecular Biology (Core) – 2.4 Proteins Name:
2.4.U1 Amino acids are linked together by condensation to form polypeptides. AND
2.4.S1 Drawing molecular diagrams to show the formation of a peptide bond.
1. Condensation of amino acids is a polymerisation reaction. A chain of amino acids joined together is
called a polypeptide. These building reactions are part of the anabolic metabolism.
a. What structure mediates and controls the formation of polypeptides?
b. Apart from the above structure what else is needed for the reaction to occur?
c. Draw and annotate a structural diagram below to outline how two generalised amino acids (i.e. use
the R-group nomenclature) into a dipeptide through condensation, producing a peptide bond.
2.4.U2 There are 20 different amino acids in polypeptides synthesized on ribosomes.
2. How many different amino acids do we know of?
http://bioknowledgy.weebly.com/ (Chris Paine)
22
3. How many of these amino acids are synthesised by ribosomes?
20
3. 2. Molecular Biology (Core) – 2.4 Proteins Name:
4. List three examples of amino acids synthesised by ribosomes.
http://bioknowledgy.weebly.com/ (Chris Paine)
5. Extension: Outline the process by which the remaining amino acids are created.
2.4.U3 Amino acids can be linked together in any sequence giving a huge range of possible polypeptides.
6. State the three key ideas that explain the huge range of possible polypeptides:
7. If a polypeptide contains just 5 amino acids calculate the how many different polypeptides can be
created.
8. State both the name of the longest polypeptide known and approximately how many amino acids it
contains.
2.4.U4 The amino acid sequence of polypeptides is coded for by genes.
9. Outline the central dogma of genetics.
4. 2. Molecular Biology (Core) – 2.4 Proteins Name:
2.4.U6 The amino acid sequence determines the three-dimensional conformation of a protein.
2.4.U5 A protein may consist of a single polypeptide or more than one polypeptide linked together.
10. The R-groups of an amino acid are classified as having one of a number of different properties. List the
properties can they possess.
http://bioknowledgy.weebly.com/ (Chris Paine)
11. Extension: complete the table to outline the four different levels of protein structure. (n.b. although you
don’t need to be able to outline the different levels of structure knowing of them helps to understand the
different functions proteins have and why)
Notes Fibrous or Globular
Primary
(polypeptide)
• The order / sequence of the amino acids of which the
protein is composed
• Formed by covalent peptide bonds between adjacent amino
acids
• Controls all subsequent levels of structure
Neither (– will fold to
become one of the
subsequent levels of
structure)
Secondary
Tertiary
Quaternary
5. 2. Molecular Biology (Core) – 2.4 Proteins Name:
12. Distinguish between globular and fibrous proteins
Fibrous Globular
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Location of
R groups
Shape
Function
Solubility
Amino acid
sequence
Stability
Examples
6. 2. Molecular Biology (Core) – 2.4 Proteins Name:
2.4.U7 Living organisms synthesize many different proteins with a wide range of functions.
13. Complete the table to describe each of different functions that proteins have in and outside of cells.
Function Description Key examples
http://bioknowledgy.weebly.com/ (Chris Paine)
Rubisco
Muscle contraction
Tubulin is the subunit of microtubules that give animals cells their
shape and pull on chromosomes during mitosis.
collagen
Blood clotting
Proteins in blood help transport oxygen, carbon dioxide, iron and
lipids.
Cell adhesion
Membrane transport
Insulin
Receptors
rhodopsin
Packing of DNA
This is the most diverse group of proteins, as cells can make huge
numbers of different antibodies.
immunoglobulins
7. 2. Molecular Biology (Core) – 2.4 Proteins Name:
2.4.A1 Rubisco, insulin, immunoglobulins, rhodopsin, collagen and spider silk as examples of the range of
protein functions.
14. Take notes to outline each of the key examples of protein function.
http://bioknowledgy.weebly.com/ (Chris Paine)
Rubisco:
insulin:
immunoglobulins:
rhodopsin:
8. 2. Molecular Biology (Core) – 2.4 Proteins Name:
http://bioknowledgy.weebly.com/ (Chris Paine)
collagen:
spider silk:
2.4.U8 Every individual has a unique proteome.
15. The proteome is unque to every individual.
a. Define the term genome.
b. Define the term proteome.
c. Aside from the genome what affects the proteome?
9. 2. Molecular Biology (Core) – 2.4 Proteins Name:
d. Explain why the proteome is larger and more varied that the genome.
2.4.A2 Denaturation of proteins by heat or by deviation of pH from the optimum.
16. Describe the term denaturation. Refer to the structure of the protein in your answer.
17. What factors can commonly cause denaturation and how?
http://bioknowledgy.weebly.com/ (Chris Paine)
Citations:
Allott, Andrew. Biology: Course Companion. S.l.: Oxford UP, 2014. Print.