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: Hemoglobin Displays Positive Cooperativity

Concept #2: Concerted & Sequential Models Explain Hb's Positive Cooperativity

Concept #3: Oxygen-Binding Curves

Concept #4: Positive Cooperativity makes Hb a Better O2 Transporter than Mb

Practice: In the binding of oxygen to myoglobin, the relationship between the concentration of oxygen and the fraction of binding sites occupied can best be described as:

Practice: Oxygen is a _____________ allosteric _____________ that promotes additional O2 binding to hemoglobin.

Practice: The binding of Oxygen to stabilize the R-state of Hemoglobin is best explained by which model(s)?