The [T] / [R] ratio is decreased and the oxygen affinity is increased.The [T] / [R] ratio is decreased and the oxygen affinity is unchanged.The [T] / [R] ratio is increased and the oxygen affinity is decreased.The [T] / [R]] ratio is increased and the oxygen affinity is increased.The [T] / [R] ratio is decreased and the oxygen affinity is decreased. The Hb Yakima variation is caused by the mutation D99H, which results in ashift in oxygen binding as shown in the graph. What effect does the D99Hvariation have on the [T] / [R] ratio of Hb Yakima protein conformationcompared to Hb Normal and how does D99H alter oxygen affinity?Fractional saturation1.02Hb Yakima20Hb Normal4060po, (kPa)80100

Hemoglobin binds to oxygen and it appears in two state. The T state (tensed) and R state (relaxed).…

Answered: The Hb Yakima variation is caused by…

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

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Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.71; Pk2 = 10.78; PkR = 8.33 His: Pk1 = 1.82; Pk2 = 9.17; PkR = 6.0 Lys: Pk1 = 2.18; Pk2 = 8.95; PkR = 10.53 draw the protonic equilibria for the tripeptide what is the IpH?
What is the approximate rate of change of A340 measured? i.e. ΔA340 / min = __________ What rate of change of A340 would you predict if 30 ml of the ADH solution was tested in the same way (i.e. half the amount of protein) ? i.e. ΔA340 / min = __________ What rate of change of A340 would you predict if 60 ml of a 0.5 μM ADH solution was tested in the same way? i.e. ΔA340 / min = __________ As well as writing your answers, explain your reasoning.
In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to the Hillcoefficient? Explain your answers.
a) What is the KDD for this myoglobin variant? b) What is the predicted fractional saturation for the last box in the table? (please show your work so I can better understand) c) What is unexpected about the binding curve above? (5 words or less) d) What must be structurally different about this new variant relative to other known Myoglobin variants to generate this graph?
The following table shows the molecular masses (Mr) and isoelectric points (pI) of five proteins: Protein Mr pI Chicken egg white lysozyme 14,000 11.0 Carbonic anhydrase 30,000 5.4 Ovalbumin 45,000 4.5 Phosphorylase b 97,000 6.7 Lactate dehydrogenase 140,000 7.12 (a) A solution containing these five proteins was adjusted to pH 7.0 and then applied to a SIZE-EXCLUSION COLUMN. Assume that these five protein molecules are spherical in shape. Which protein is likely to be eluted LAST from the column? Explain briefly. (b) In another experiment, this protein mixture was first adjusted to pH 6.7 before applying to a CATION-EXCHANGE COLUMN. (i)What is the net charge on phosphorylase b? (ii) Which of these five proteins will bind to the CATION-EXCHANGER? Explain briefly.v
Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.71; Pk2 = 10.78; PkR = 8.33 His: Pk1 = 1.82; Pk2 = 9.17; PkR = 6.0 Lys: Pk1 = 2.18; Pk2 = 8.95; PkR = 10.53 What is the dominant structure at pH 2.0? What is the first buffering region of the tripeptide?
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?
In oxygenated hemoglobin, pKa 5 6.6 forthe histidines at position 146 on the -chain. In deoxygenated hemoglobin, the pKa of these residues is 8.2. How can this piece ofinformation be correlated with the Bohr effect?
In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These messages yielded proteinswith the amino acid compositions shown in the followingtable. Using these data, predict the most specific coding compositionfor each amino acid.4/5C:1/5A 4/5A:1/5CPro 63.0% Pro 3.5%His 13.0% His 3.0%Thr 16.0% Thr 16.6%Glu 3.0% Glu 13.0%Asp 3.0% Asp 13.0%Lys 0.5% Lys 50.0% 98.5% 99.1%
You want to treat 10 mL of HL-60 cells with cycloheximide in order to determine the half-life of a newly discovered protein. In order to do this, the final concentration of cycloheximide needs to be 90 µM. How much of a 150 mM stock solution of cycloheximide should you add to your cells?
A protein sample of unknown concentration was placed in a cuvette with a path length of 1 cm and the sample was found to have an A280 value of 2.92. If the protein of interest has an extinction coefficient of 44240 M-1 cm-1 and the molecular weight of the protein is 47.411 kDa, what is the concentration of protein in mg/mL?
What is the molecular weight of the Botulinum neurotoxin, a protein that contains 1350 amino acids? Assume an average distribution of amino acids

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