Given below is the electrophoretic profile of 2 proteins, a normal hemoglobin, HbA and the fetal hemoglobin, HbF. What information can be obtained from the profile shown? (+) HbF ww wm (-) HbA A. HbF has a slightly different conformation compared with HbA B. HbF and HbA have different primary structures C. HbF has a higher affinity for oxygen than HbA D. HbF has a nonpolar amino acid residue in place of a basic amino acid. E. HbF has an acidic amino acid residue in place of a nonpolar amino acid

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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Given below is the electrophoretic profile of 2 proteins,
a normal hemoglobin, HbA and the fetal hemoglobin,
HbF. What information can be obtained from the profile
shown?
wwwwwww
(+)
HbF
ww w
(-)
HbA
ww ww
A. HbF has a slightly different conformation compared with
HbA
B. HbF and HbA have different primary structures
C. HbF has a higher affinity for oxygen than HbA
D. HbF has a nonpolar amino acid residue in place of a basic
amino acid.
E. HbF has an acidic amino acid residue in place of a
nonpolar amino acid
Transcribed Image Text:Given below is the electrophoretic profile of 2 proteins, a normal hemoglobin, HbA and the fetal hemoglobin, HbF. What information can be obtained from the profile shown? wwwwwww (+) HbF ww w (-) HbA ww ww A. HbF has a slightly different conformation compared with HbA B. HbF and HbA have different primary structures C. HbF has a higher affinity for oxygen than HbA D. HbF has a nonpolar amino acid residue in place of a basic amino acid. E. HbF has an acidic amino acid residue in place of a nonpolar amino acid
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