Imagine there is a beaker with a solution containing 1,000 hemoglobin homotetramers and 1,000 protons (H*). Which of the statementsconcerning the concerted and sequential models is NOT true if you assume only 1 proton is capable of binding 1 hemoglobin monomer?Select one:a. If an additional 1,000 protons were added, according to the concerted model, all of the homotetramers will adopt the R state.b. According to the concerted model, the addition of protons will cause an increase in the number of tetramers in the T state.c. According to the sequential model, there will be some monomers of homotetramers in the R state and some in the T state.d. If an additional 2,000 protons were added, according to the sequential model, there will be a greater proportion of hemoglobin inthe T state.е.If an additional 2,000 protons were added, according to the concerted model, more hemoglobin will adopt the T state.

Hemoglobin is a protein found in the red blood cells that are involved in the transport of carbon…

Answered: Imagine there is a beaker with a…

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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How many hemoglobin molecules are there in an average red cell? Assume that the molecular weight of the human hemoglobin tetramer is 65 kDa.
It is speculated that, in 1954, the scientist Allan Turing (who was instrumental in decoding the German Enigma code during the Second World War) ate an apple, which had been injected with a solution of cyanide, to commit suicide. How does cyanide poisoning work on a molecular level, and why can this type of toxic effect not be prevented as in the case of methanol poisoning?
Consider olive oil, an oil with a high percentage of fat derived from oleic acid (otherwise known as cis[18:1] fatty acid). a, Explain why such a structure may allow olive oil to be one of the "healthier" oils? b, why such a structure may allow olive oil to be a liquid at room temperature, while butter and lard are solid at room temperature? c, why such a structure may cause olive oil to be prone to oxidative damage upon exposure to air and heat?
At a pH equal to the isoelectric point of alanine, the net charge on alanine is zero. Two structures can be drawn that have a net charge of zero, but the predominant form of alanine at its pI is zwitterionic.(a) Why is alanine predominantly zwitterionic rather than completely uncharged at its pI?(b) What fraction of alanine is in the completely uncharged form at its pI? Justify your assumptions.
Draw Ramachandran plot for: a) regular secondary structure with Φ = 60-65 and Ψ = 60-80 b) regular secondary structure with Φ = -170 and Ψ = 170 c) intrinsically disordered proteins d) explain why these Ramachsndran plots will be different, and what secondary structures are described in A and in B
Assume that some protein molecule, in its folded native state, has one favored conformation. But when it is denatured, it becomes a “random coil,” with many possible conformations. (a) If we only consider the change in entropy for the protein, what must be the sign of ∆S for the change: native → denatured? (Note: As suggested in the next problem, this does not include solvent effects, which also make significant contributions to ∆S.) (b) How will the contribution of ∆S for native → denatured affect the favorability of the process? What apparent requirement does this impose on ∆H if proteins are to be stable structures?
You have an initial solution in which you added quantities of “A” and “B” such that there is 4.5 M “A” and 2.5 M “B” and no complex (“AB”) at time 0. After equilibrium, you are able to isolate and quantitate the “AB” complex, and find its concentration is 1.5 M. Given that RT is 0.59 kcal/mol, what is the delta Go’ for the association reaction?
Assume that some protein molecule, in its folded native state, has onefavored conformation. But when it is denatured, it becomes a “random coil,” with many possible conformations.(a) If we only consider the change in entropy for the protein, what mustbe the sign of ΔS for the change: native → denatured? (Note: As suggestedin the next problem, this does not include solvent effects, which also make significant contributions to ΔS.)(b) How will the contribution of ΔS for native → denatured affect thefavorability of the process? What apparent requirement does this imposeon ΔH if proteins are to be stable structures?
1)Ubiquitin is a small protein with a monoisotopic mass of 8560 Da. a) Electrospray ionization of this small protein typically results in major charge states of +8, +9, +10, +11, +12, and +13. Using this information, complete the table below, assuming the charges on each come from protonation. Report mass and m/z values to the ones place. b) Using the data you entered in the table, sketch an expected ESI-MS spectrum for ubiquitin. Label each peak with its charge state. What do you notice about the spacing of peaks along the x-axis. c)The figure shows an experimentally obtained electrospray mass spectrum for ubiquitin. Compare this spectrum to the spectrum you predicted. Are there any differences? If so, what might cause these differences?
The following data describe binding of ligand A to a protein, using both Scatchard plots and Hills plots, tell as much as you can about the binding reaction. [A](M) 1X10-6 5 X10-6 1 X10-5 5 x 10-5 1 X 10-4 5 x 10-4 1x 10-3 5X10-3 ṽ 0.101 0.381 0.591 1.116 1.409 1.813 1.899 1.955..
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.
Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.5; Pk2 = 10.8; PkR = 8.5 His: Pk1 = 1.6; Pk2 = 9.0; PkR = 7.0 Lys: Pk1 = 2.2; Pk2 = 8.5; PkR = 9.8 a.draw the protonic equilibria for the tripeptide. b.what is the IpH? c.What is the dominant structure at pH 3.0? d.What is the first buffering region of the tripeptide?

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