Amino Acids and Protein Primary Structure
Students will learn about the complex structure and vast array of functions of proteins, from enzymes to structural components, emphasizing their importance in all life processes.
Key Questions
- Explain how the R-group chemistry of amino acids (nonpolar, polar uncharged, positively charged, negatively charged) determines their contribution to protein folding, active site interactions, and post-translational modification.
- Apply your knowledge of protein primary structure to predict the consequence on enzyme function of a missense mutation that substitutes a charged active-site residue with a hydrophobic one, referencing the effect on substrate binding and catalysis.
- Evaluate how SDS-PAGE gel electrophoresis and the biuret test can be used together to detect a specific protein in a cell extract and estimate its molecular mass, identifying the assumptions and limitations of each technique.
MOE Syllabus Outcomes
Suggested Methodologies
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