Chem 4320/5320: Biochemistry 1
- Page ID
- 165250
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Front Matter
1: Properties of the Twenty Common Amino Acids
2: Proteins Structure: from Amino Acid Sequence to Three Dimensional Structure
3: Methods of Protein Purification and Characterization
4: Overview of Hemoglobin and Myoglobin
5: Michaelis-Menten Enzyme Kinetics, Inhibitors, pH optima; Bi-Substrate Reactions
6: Classification and Catalytic Strategies of Enzymes
8: Carbohydrate Structures, Stereochemistry, and Glycosides
11: Electron Transport Chain and Oxidative Phosphorylation
Back Matter
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). (CC BY 4.0; Thomas Shafee).