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.
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
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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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.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F23c38651-d5a3-4c38-ab9e-97c20b9d1405%2Fec9aec2f-7b46-431a-8bec-30bb9cf7d86e%2Fe1z1krv_processed.png&w=3840&q=75)
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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