Protein Conformation: Secondary to Quaternary Structure and Denaturation
Students will be introduced to DNA and RNA, understanding their fundamental roles in storing, transmitting, and expressing genetic information.
Key Questions
- Explain how intramolecular forces — hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges — stabilise each level of protein structure, and predict which bonds are disrupted when pH or temperature is altered.
- Compare the structural features of a fibrous protein such as collagen with a globular protein such as haemoglobin, relating each structural feature to its specific biological function.
- Evaluate the evidence that protein denaturation can be reversible under mild conditions and explain how molecular chaperones assist newly synthesised polypeptides in achieving their native tertiary conformation in vivo.
MOE Syllabus Outcomes
Suggested Methodologies
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