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Protein Structure: Group Based Learning Learning Objectives

This document outlines a group learning activity on protein structure where students will research and answer questions in small groups about the building blocks, levels of structure, forces that determine structure, and how environmental changes can alter protein conformation. The questions cover topics like amino acid composition, primary/secondary/tertiary structure, protein denaturation, essential amino acids, and examples of specific protein structures and functions.

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46 views3 pages

Protein Structure: Group Based Learning Learning Objectives

This document outlines a group learning activity on protein structure where students will research and answer questions in small groups about the building blocks, levels of structure, forces that determine structure, and how environmental changes can alter protein conformation. The questions cover topics like amino acid composition, primary/secondary/tertiary structure, protein denaturation, essential amino acids, and examples of specific protein structures and functions.

Uploaded by

kxng crocked
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd
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Protein Structure

Group Based Learning

Learning Objectives:
Identify the amino acid constituents of proteins
Describe the four levels of protein structure
Explain the forces which determine the folded structure of proteins
Explain how ligand binding and environmental changes can reversibly alter the
conformational states of proteins
Recognise the limits of structural stability of proteins and explain the process of
denaturation

Instructions:
- Students should work within their PBL groups to research, discuss, answer the
following questions.
- In a collaborative space (PBL Teams – Class Notebook),
- All students within each group should input in the discussion via Teams Chat (could
schedule discussion time). Instructor to review chat for individual contributions.
- Students to present answers on Thursday 23rd September 2021 plenary
- Answers to the questions should be posted by Friday 24th September 2021 in the
Collaborative space for all the class to view – (SOM201 – Class Notebook/Files)

Questions are assigned as:


PBL Group A - QUESTIONS 1 & 2
PBL Group B - QUESTIONS 3 to 8
PBL Group C - QUESTIONS 9 to 11
PBL Group D - QUESTIONS 12 to 14
PBL Group E - QUESTIONS 15 to 19*
PBL Group F - QUESTIONS 20 to 23
PBL Group G - QUESTIONS 24 to 25 (Myosin, CD4, Albumin, Keratin)
PBL Group H - QUESTIONS 24 to 25 (Immunoglobulin-G, Reverse transcriptase,
Haemoglobin and, insulin)
PBL Group I - QUESTIONS 15 to 19 *
Questions:

Importance of proteins in living organisms.


1. What are proteins? How can the protein diversity of living beings be explained?
2. What is the importance of proteins for living organisms?

Basic Units of Proteins.


3. What is the constitutional unit of proteins? Briefly describe the basic structure of
proteins?
4. What is an oligopeptide? How is it different from a polypeptide?
5. Generally, how many amino acids that form proteins in living organisms?
6. Does every amino acid have a central carbon? To which organic group is that central
carbon bound?
7. What is the structural representation of carboxyl group?
8. What is the importance of the -R group (variable radical) in amino acid molecule?
Peptide Bond Formation.
9. Describe bond formation between two amino acids
10. What is this type of bond formation called?
11. Does the bond formation incorporate or liberate atoms? If so, what
compound/molecule is incorporated or liberated in this reaction?

Amino Acid Sequence Conservation and Protein Synthesis.


12. Can the same total number of amino acids make different proteins?
13. Are proteins with the same number of each different amino acid that form them
necessarily be identical proteins?
14. What is the essential condition for a protein to be identical to another protein?

Levels of Protein Structure.


15. Describe the primary structure of a protein? What is the significance of this
structure?
16. How is the secondary protein structure generated?
17. Delineate the difference(s) between the alpha-helix and the beta-sheet protein
conformations.
18. Describe the tertiary protein structure. What are the main types of tertiary
structure?
19 Explain what quaternary protein structure is.
a. Do all proteins have a quaternary structure?
b. Give details of bond(s) associated with folded protein structure.

Protein Denaturation.
20. What is protein denaturation? Is there any change in the primary protein structure
when a protein is denatured?
21. How can protein denaturation be classified regarding its reversibility?
22. List factors that can lead to protein denaturation.
23. Are there a functional consequence of changes in Primary/Secondary/Tertiary
Structures?
a. What are the effects of the changes?
b. Give examples of instances/diseases where all the structural levels of the
protein is affected and how these changes occurred. What is the impact of
these changes in the particular example.

Essential Amino Acids.


24. Describe what essential amino acids are. List all the essential amino acids.

Examples and Functions of Varying Proteins.


25. Briefly describe the structures of the following proteins and enumerate some of
their remarkable functions:
Myosin, CD4, Albumin, Keratin, Immunoglobulin G, Reverse transcriptase,
Haemoglobin and, insulin.

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