Sections
Introduction to Protein-Ligand Interactions
Protein-Ligand Equilibrium Constants
Protein-Ligand Fractional Saturation
Myoglobin vs. Hemoglobin
Heme Prosthetic Group
Hemoglobin Cooperativity
Hill Equation
Hill Plot
Hemoglobin Binding in Tissues & Lungs
Hemoglobin Carbonation & Protonation
Bohr Effect
BPG Regulation of Hemoglobin
Fetal Hemoglobin
Sickle Cell Anemia
Chymotrypsin
Chymotrypsin's Catalytic Mechanism
Glycogen Phosphorylase
Liver vs Muscle Glycogen Phosphorylase
Antibody
ELISA
Motor Proteins
Skeletal Muscle Anatomy
Skeletal Muscle Contraction

Concept #2: Chymotrypsin's Active Site

Practice: Which amino acids in chymotrypsin’s active site are critical participants in the cleavage of the substrate?

Practice: The following polypeptide N-G-I-F-D-A-Y-G-N-T-W-R-A-P-C-F-V-A is cleaved by chymotrypsin to produce multiple peptide fragments. Based on the specificity of chymotrypsin cleavage, how many peptide fragments are produced?

Practice: The activity of chymotrypsin drastically changes as the pH fluctuates in the relatively small range of pH 5-9. What amino acid residue in chymotrypsin’s active site is most likely to be responsible for this effect of pH?