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Allosteric Effects(Biochemistry ) Questions and Answers
Home
Topic
Biochemistry
Allosteric Effects
Question 1.
The conformational changes from the T to the R state is initiated by
reorganization of protein-protein contacts between the individual subunits
movement of the F-helix, which contains the proximal His
binding of oxygen to the heme
movement of the proximal histidine towards the heme
Explanation:-
Answer: Option C. ->
binding of oxygen to the heme
Question 2.
Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because
it is displaced from the heme by oxygen
its binding pocket becomes too small to accommodate BPG
it is displaced from the heme by movement of the proximal histidine
BPG binds to the R state with the same affinity as the T state
Explanation:-
Answer: Option B. ->
its binding pocket becomes too small to accommodate BPG
Question 3.
An allosteric activator
both (a) and (c)
decreases the binding affinity
stabilizes the R state of the protein
increases the binding affinity
Explanation:-
Answer: Option A. ->
both (a) and (c)
Question 4.
When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is
2
1
not defined
None of these
Explanation:-
Answer: Option A. ->
2
Question 5.
The Hill coefficient (nH) for myoglobin and hemoglobin are respectively
1.2 and 4.5
1.0 and 2.8
2.8 and 1.0
4.5 and 1.2
Explanation:-
Answer: Option B. ->
1.0 and 2.8
Question 6.
Small molecules affect hemoglobin (Hb) by
decreasing Hb affinity for O2
increasing [H+]
increasing Hb affinity for O2
increasing [H+] and decreasing Hb affinity for O2
Explanation:-
Answer: Option D. ->
increasing [H+] and decreasing Hb affinity for O2
Question 7.
In hemoglobin, allosteric effects occur
for maintaining Fe in the Fe2+ state
to minimize oxygen delivery to the tissues
only in humans
to maximize oxygen delivery to the tissues
Explanation:-
Answer: Option D. ->
to maximize oxygen delivery to the tissues
Question 8.
A protein that shows infinite cooperative for binding of n ligands will
only be found in either the unliganded form or the fully liganded form
show a Hill coefficient (nH) of 0.0
both (b) and (c)
show a Hill coefficient (nH) of n
Explanation:-
Answer: Option C. ->
both (b) and (c)
Question 9.
A protein that binds two ligands in a non-cooperative manner will show
a hyperbolic binding curve
a sigmodial binding curve
both (b) and (c)
a linear Scatchard Plot
Explanation:-
Answer: Option C. ->
both (b) and (c)
Question 10.
O2 binding to hemoglobin results in
100-fold lower affinity for the last O2 bound than for the first
both (a) and (b)
extensive protein conformational change
100-fold higher affinity for the last O2 bound than for the first
Explanation:-
Answer: Option B. ->
both (a) and (b)
1
2
3
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