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,...
icon
Related questions
Question
. 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.
Expert Solution
trending now

Trending now

This is a popular solution!

steps

Step by step

Solved in 2 steps

Blurred answer
Similar questions
Recommended textbooks for you
Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
Anatomy and Physiology
ISBN:
9780134580999
Author:
Elaine N. Marieb, Katja N. Hoehn
Publisher:
PEARSON
Anatomy & Physiology
Anatomy & Physiology
Anatomy and Physiology
ISBN:
9781259398629
Author:
McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:
Mcgraw Hill Education,
Human Anatomy
Human Anatomy
Anatomy and Physiology
ISBN:
9780135168059
Author:
Marieb, Elaine Nicpon, Brady, Patricia, Mallatt, Jon
Publisher:
Pearson Education, Inc.,
Anatomy & Physiology: An Integrative Approach
Anatomy & Physiology: An Integrative Approach
Anatomy and Physiology
ISBN:
9780078024283
Author:
Michael McKinley Dr., Valerie O'Loughlin, Theresa Bidle
Publisher:
McGraw-Hill Education
Human Anatomy & Physiology (Marieb, Human Anatomy…
Human Anatomy & Physiology (Marieb, Human Anatomy…
Anatomy and Physiology
ISBN:
9780321927040
Author:
Elaine N. Marieb, Katja Hoehn
Publisher:
PEARSON