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Biochemistry - Allosteric Effects

Exercise : Allosteric Effects - Section 1
  • Allosteric Effects - Section 1
1.
The conformational changes from the T to the R state is initiated by
binding of oxygen to the heme
movement of the proximal histidine towards the heme
movement of the F-helix, which contains the proximal His
reorganization of protein-protein contacts between the individual subunits
Answer: Option
Explanation:
No answer description is available. Let's discuss.
2.
An allosteric activator
increases the binding affinity
decreases the binding affinity
stabilizes the R state of the protein
both (a) and (c)
Answer: Option
Explanation:
No answer description is available. Let's discuss.
3.
Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because
it is displaced from the heme by oxygen
it is displaced from the heme by movement of the proximal histidine
its binding pocket becomes too small to accommodate BPG
BPG binds to the R state with the same affinity as the T state
Answer: Option
Explanation:
No answer description is available. Let's discuss.
4.
The Hill coefficient (nH) for myoglobin and hemoglobin are respectively
2.8 and 1.0
1.0 and 2.8
1.2 and 4.5
4.5 and 1.2
Answer: Option
Explanation:
No answer description is available. Let's discuss.
5.
When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is
1
2
not defined
none of the above
Answer: Option
Explanation:
No answer description is available. Let's discuss.
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