EXPLAIN your choices for each of the following: a) The Hb variant least likely to cause pathological symptoms b) The variant(s) most likely to show pl values different from that of HbA c) The variant(s) most likely to show a decrease in BPG binding and an increase in the overall affinity of the Hb's oxygen affinity.
EXPLAIN your choices for each of the following: a) The Hb variant least likely to cause pathological symptoms b) The variant(s) most likely to show pl values different from that of HbA c) The variant(s) most likely to show a decrease in BPG binding and an increase in the overall affinity of the Hb's oxygen affinity.
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
Problem 1P
Related questions
Question
1. Hemoglobin researchers have discovered more than 500 naturally occurring hemoglobin mutations. The majority of these results from single amino acid changes. Some of these mutations result in clinical illness or symptoms, but many show no outward effects. Some examples are:
HbS (sickle cell Hb)-substitutes Val for Glu on the surface
Hb Cowtown - eliminates an ion pair used in T-state stabilization
Hb Memphis - surface uncharged polar aa for another of similar size on the surface
Hb Bibba-substitutes a Pro for a Leu in an α-helix
Hb Milwaukee - substitutes a Glu for a Val
Hb Providence- substitutes a Asn for a Lys that normally projects into the central cavity
Hb Philly - substitutes a Phe for a Tyr, disrupting hydrogen bonding at the aß interface.
EXPLAIN your choices for each of the following:
a) The Hb variant least likely to cause pathological symptoms
b) The variant(s) most likely to show pl values different from that of HbA
c) The variant(s) most likely to show a decrease in BPG binding and an increase in the overall affinity of the Hb's oxygen affinity.
2. What effect does each of the following treatments have on the oxygen affinity of hemoglobin A in vitro?
a. dissociation of the tetramer complex into separate monomer subunits
b. decrease in CO2 from 20 to 5 torr
Expert Solution
This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
This is a popular solution!
Trending now
This is a popular solution!
Step by step
Solved in 4 steps
Recommended textbooks for you
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON