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

Practice: Identify all the correct statements regarding the Bohr effect on hemoglobin.

i) The Bohr effect shifts the fractional O2 saturation curve to the right as pH decreases.

ii) The Bohr effect shifts the fractional O2 saturation curve to the right as pH increases.

iii) The Bohr effect favors O2 release in respiring tissues.

iv) O2 and H+ compete for the same binding site on hemoglobin.

Concept #2: Summary of the Bohr Effect

Practice: On the graph below, draw in the approximate shapes of the O 2-saturation curves in the lungs & tissues after a shift due to the Bohr effect takes place.

Practice: The Bohr effect describes the change in hemoglobin’s affinity for oxygen under two different conditions. What are these two conditions and how do they impact hemoglobin’s affinity for oxygen? Complete the table below: