Question is ⇒ In hemoglobin, allosteric effects occur, Options are ⇒ (A) only in humans, (B) for maintaining Fe in the Fe<sup>2+</sup> state, (C) to minimize oxygen delivery to the tissues, (D) to maximize oxygen delivery to the tissues, (E) , Leave your comments or Download question paper.

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Question is ⇒ In hemoglobin, allosteric effects occur, Options are ⇒ (A) only in humans, (B) for maintaining Fe in the Fe<sup>2+</sup> state, (C) to minimize oxygen delivery to the tissues, (D) to maximize oxygen delivery to the tissues, (E) , Leave your comments or Download question paper. Previous question Next question


Q1.	In hemoglobin, allosteric effects occur
A.	only in humans [Wrong Answer]
B.	for maintaining Fe in the Fe²⁺ state [Wrong Answer]
C.	to minimize oxygen delivery to the tissues [Wrong Answer]
D.	to maximize oxygen delivery to the tissues [Correct Answer]
View Answer 10 -4 Explanation:- Answer : D Discuss it below : !! OOPS Login [Click here] is required to post your answer/result Help other students, write article, leave your comments

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⇒ 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

⇒ A protein that binds two ligands in a non-cooperative manner will show
a sigmodial binding curve
a hyperbolic binding curve
a linear Scatchard Plot
both (b) and (c)

⇒ The specificity of a ligand binding site on a protein is based on
the absence of competing ligands
the amino acid residues lining the binding site
the presence of hydrating water molecules
the opposite chirality of the binding ligand

⇒ In hemoglobin, allosteric effects occur
only in humans
for maintaining Fe in the Fe²⁺ state
to minimize oxygen delivery to the tissues
to maximize oxygen delivery to the tissues

⇒ An allosteric activator
increases the binding affinity
decreases the binding affinity
stabilizes the R state of the protein
both (a) and (c)

⇒ O₂ binding to hemoglobin results in
100-fold higher affinity for the last O₂ bound than for the first
extensive protein conformational change
both (a) and (b)
100-fold lower affinity for the last O₂ bound than for the first

⇒ 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

⇒ 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

⇒ A protein that shows infinite cooperative for binding of n ligands will
show a Hill coefficient (n_H) of 0.0
only be found in either the unliganded form or the fully liganded form
show a Hill coefficient (n_H) of n
both (b) and (c)

⇒ 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

⇒ The Hill coefficient (n_H) 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

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