GENETIC ANALYSIS: AN INTEG. APP. W/MAS
2nd Edition
ISBN: 9781323142790
Author: Sanders
Publisher: Pearson Custom Publishing
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Chapter 10, Problem 8P
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When human hemoglobin undergoes a mutation, the
mutant protein usually does not replace all of the normal HbA in
the red blood cells or erythrocytes of the individual. The erythro-
cytes contain mixtures of varying amounts of both HbA and the
mutant protein depending on the mutation and the individual. Hb
Yakima is a mutant human Hb with an Asp-(B99)His mutation.
The diagram on the right shows that Hb Yakima was separated
by DEAE-cellulose chromatography from HbA with a 0 – 0.1 M
linear gradient of NaCl buffered to pH 8.3. Why is chromatog-
raphy carried out at pH 8.3? If the isoelectric point of HbA is 6.85,
what is the change in total charge caused by the mutation?How
does the change in charge explain the chromatography elution
profile of the Hb Yakima/HbA mixture?
1,5
-Hb-A
Hb -Yakima
1.0
0.5-
20
40
60
80
00
Fraction number
O.D578 nm
Below is the DNA base sequence for the normal protein for normal hemoglobin and the base sequence for (abnormal) sickle cell hemoglobin:
Normal GGG CTT CTT TTT
Sickle GGG CAT CTT TTT
A)Transcribe and translate the normal and sickle cell DNA.
B)Identify this as a point or frameshift mutation. Explain.
The proximal histidine residues have been replaced by glycine residues by mutation of the cloned genes for both the α and β subunits of hemoglobin. With the tetrameric mutant hemoglobin (all subunits being mutant, α H F8 G, β H F8 G), it was found that the “proximal” coordination bonds to hemes in the mutant protein could be replaced by having the small molecule imidazole in the buffers. Oxygen binding curves for the tetrameric mutant hemoglobin were measured.
A. The degree of cooperativity in oxygen binding for the mutant hemoglobin (with imidazole present) would be expected to
1) increase 2) decrease 3) not be affected)
compared with the normal protein.
B. Justify your answer to part A in terms of what you know about the structural basis of cooperativity in hemoglobin.
C. How would the Hill coefficient for the mutant be expected to change compared with nH for normal hemoglobin, which is ~3?
Chapter 10 Solutions
GENETIC ANALYSIS: AN INTEG. APP. W/MAS
Ch. 10 - Define the following terms as described in this...Ch. 10 - 2. Using sickle cell disease as an example,...Ch. 10 -
3. Compare and contrast the contributions of...Ch. 10 - Why do differences in protein electrophoretic...Ch. 10 - Prob. 5PCh. 10 - Prob. 6PCh. 10 - Prob. 7PCh. 10 - 8. Wildtype βglobin protein is composed of amino...Ch. 10 - Prob. 9PCh. 10 - Prob. 10P
Ch. 10 - 11. How is an autoradiograph produced from a...Ch. 10 - Prob. 12PCh. 10 - Prob. 13PCh. 10 - Prob. 14PCh. 10 - The family represented in the pedigree and...Ch. 10 - Suppose the mating couple (I-1 and I-2) shown in...Ch. 10 - What are restriction endonucleases, and why are...Ch. 10 - 18. Following restriction digestion, DNA fragments...Ch. 10 - 19. The doublestranded DNA sequence below is part...Ch. 10 - 20. Restriction enzymes recognize specific...Ch. 10 - Prob. 21PCh. 10 - Prob. 22PCh. 10 - Prob. 23PCh. 10 - Prob. 24PCh. 10 - 25. A second strain of dwarf plants has a...Ch. 10 - During gel electrophoresis of linear DNA...Ch. 10 - Prob. 27PCh. 10 - 28. In molecular biology, restriction...Ch. 10 - A complete plant gene containing four introns and...Ch. 10 - Prob. 30PCh. 10 - The map below illustrates three alleles in a...Ch. 10 - Prob. 32PCh. 10 - 33. Northern blot analysis is performed on mRNA...
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