Ch. 6 Flashcards
What are the structural differences between myoglobin & hemoglobin?
- Myoglobin: single polypeptide chain with 1 heme group
- Hemoglobin: 4 polypeptides with 2 alpha and 2 beta subunits
What is fractional saturation?
The fraction of protein binding sites that are occupied
What is the formula for fractional saturation?
[protein-ligand complex]/[protein-ligand complex]+[protein]
What is the Bohr effect?
pH and CO2 dependence of oxygen binding
Where is 2,3-bisphosphoglycerate?
RBCs
What does 2,3-bisphosphoglycerate do?
Traps hemoglobin the the T state and acts as a negative effector
Where are positive regulators graphed?
To the left
How does 2,3-BPG affect oxygen binding?
Binding of 2,3-BPG to a secondary site inhibits binding of O2 to the primary sites
Where does 2,3-bisphosphoglycerate bind?
Between the 2 beta subunits
Why does 2,3-BPG prefer to bind to the T state of Hb?
R state of Hb has a smaller central cavity
What stabilizes the binding of 2,3-BPG to the beta subunits?
Ionic interactions between 2,3-BPG and 3 positively charges residues on each beta subunit
What is the effect of amino acid differences between adult and fetal hemoglobin?
- Reduces the affinity of 2,3-BPG for the α2γ2 complex (fetus) compared to its affinity for the normal adult α2β2 complex
- Decrease in 2,3-BPG affinity facilitates transfer of O2 from the mom’s Hb to the fetal Hb because fetal Hb can get more O2 if more Hb molecules are in the R-state (high-affinity)
List membrane proteins.
- Membrane receptor proteins
- Membrane-bound metabolic enzymes
- Membrane transport proteins
What do membrane receptor proteins do?
Signal transduction
What do membrane-bound metabolic enzymes do?
Involved in redox reactions and ATP synthesis