The mutation in hemoglobin at B82 Lys → Asp results in lowered 02-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site. A rationale for the observed reduction in O2-binding affinity is: A. The positive charge on the Asp side chain can form salt bridges with other negative charged side chains stabilizing R-conformer. B. The negative charge on the Asp side chain can form salt bridges with other positive charged side chains stabilizing the T-conformer. C. The Asp side chain mimics the positive charge on BPG. D. The Asp side chain mimics the negative charge on BPG. E. The Asp side chain is a nucleophile that attacks the BPG. BPG attacks the Asp side chain. G. Stabilization of the R-conformer favors 0, release. H. Stabilization of the T-conformer favors 0, release. F.

Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
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Chapter1: The Human Body: An Orientation
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. The mutation in hemoglobin at B82 Lys → Asp results in lowered O2-binding affinity compared
to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site. A
rationale for the observed reduction in O2-binding affinity is:
A. The positive charge on the Asp side chain can form salt bridges with other negative charged
side chains stabilizing R-conformer.
B. The negative charge on the Asp side chain can form salt bridges with other positive charged
side chains stabilizing the T-conformer.
C. The Asp side chain mimics the positive charge on BPG.
D. The Asp side chain mimics the negative charge on BPG.
E. The Asp side chain is a nucleophile that attacks the BPG.
F.
BPG attacks the Asp side chain.
G. Stabilization of the R-conformer favors O, release.
H. Stabilization of the T-conformer favors O, release.
Transcribed Image Text:. The mutation in hemoglobin at B82 Lys → Asp results in lowered O2-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site. A rationale for the observed reduction in O2-binding affinity is: A. The positive charge on the Asp side chain can form salt bridges with other negative charged side chains stabilizing R-conformer. B. The negative charge on the Asp side chain can form salt bridges with other positive charged side chains stabilizing the T-conformer. C. The Asp side chain mimics the positive charge on BPG. D. The Asp side chain mimics the negative charge on BPG. E. The Asp side chain is a nucleophile that attacks the BPG. F. BPG attacks the Asp side chain. G. Stabilization of the R-conformer favors O, release. H. Stabilization of the T-conformer favors O, release.
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