BIS 102: Structure and Function of Biomolecules (Gasser)
- Page ID
- 6083
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Structure and function of macromolecules with emphasis on proteins, catalysis, enzyme kinetics, lipids, membranes, and proteins as machines.
1: Intro to Biochemistry, H2O properties, and Biochemical bonds
- 2: Biochemical Bonds, Free energy,
- 3: H2O dissociation, pH, Weak Acids and Bases
- 4: Buffers, Polyprotic acids; Amphoteric Substances,
5: Amino Acid Structure, Function
- 6: Amino Acid Separation, Peptide Bonds, and Protein Sequencing
- 7: Protein Structure
- 8: Protein Structure, Self assembly – Multimeric Proteins, Cytoskeletal fibers, Protein Evolution
- 9: Self assembly – Lipids, Membranes
- 10: Protein purification
- 11: Binding proteins- Antibodies, Myoglobin/Hemoglobin
- 12: Hemoglobin and allosteric effects
- 13: Enzymes/Catalysis
- 14: Mechanisms of Catalysis – Serine proteases, Enzyme modification, Ribozymes
- 15: Ribozymes, Enzyme Kinetics
- 16: Enzyme Kinetics, Inhibitor Kinetics
- 17: Inhibitor Kinetics (cont.), Sigmoidal kinetics, Enzyme Activation
- 18: Dynamics of Cytoskeletal Fibers, Motor Proteins
- Reader
Thumbnail: An enzyme binding site that would normally bind substrate can alternatively bind a competitive inhibitor, preventing substrate access. Dihydrofolate reductase is inhibited by methotrexate which prevents binding of its substrate, folic acid. Binding site in blue, inhibitor in green, and substrate in black(PDB: 4QI9). Image used with permission (CC BY 4.0; Thomas Shafee).