Deoxyhemoglobin's structure is stabilized by various interactions except for : A. BPG binding
What is the Deoxyhemoglobin's structure?
Deoxyhemoglobin's structure is stabilized by various interactions, including salt bridges between acidic and basic side chains, coordination of hemes with distal histidine, hydrophobic interactions, and salt bridges involving N-terminal carbamates.
However, binding of 2,3-bisphosphoglycerate (BPG) destabilizes the deoxyhemoglobin structure, promoting the release of oxygen. BPG reduces the affinity of hemoglobin for oxygen, allowing oxygen to be more readily released in tissues where it is needed.
The answer is: A. BPG binding.
Complete Questions:
The structure of deoxyhemoglobin is stabilized by each of the following interactions except:
A. BPG binding
B. salt bridges between acidic and basic side chains
C. Coordination of the hemes with the distal histidine
D. hydrophobic interactions
E. salt bridges involving N-terminal carbamates