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 #1: Why is the Heme Group on Hb/Mb Important?

Concept #2: Structure of Heme

Concept #3: Structure of Heme 

Concept #4: Interactions of Fe2+ In the Heme

Practice: When O2 binds to a heme group, the two bonds of Fe2+ that are not planar with the heme are occupied by:

Concept #5: Myoglobin's Heme Interactions

Practice: The distal histidine residue in myoglobin acts to:

Concept #6: Heme O2's Binding Causes Conformational Changes

Practice: In hemoglobin, the equilibrium transition from T state to R state is triggered by: