6. For a 1:1 ligand-receptor binding interaction that is modeled by X + Y XY :(A)Show how the fraction of ligand-receptor binding (fo) is represented by the[X][X]+ K,equation of f,(i.e., derive this expression for this reaction beginningegwith the relationship for K = f([X].[X],[XY]) under equilibrium conditions).(B)shown to the right for thisreaction, what is theestimated value of Keg? Giveyour answer in units of M.For the data plot0.90.80.70.6문 0.50.40.30.20.10.0000 0.0050 0.0100 0.0150 0.0200 0.0250 0.0300 0.0350 0.0400[X) (mM)

Lets consider the equilibrium reaction; X + Y ⇌KdKa XY Here 'X' is the ligand, 'Y' is the receptor…

Answered: 6. For a 1:1 ligand-receptor binding…

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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During an SAR effort to identify tyrosine kinase inhibitors, it was found that compound 2 was significantly more potent and selective than compound 1. To what might you attribute this improvement in activity and selectivity? Explain. IC-5 micromolar IC-0.1 mromolar
2. The following tyrosine-phosphorylated polypeptides were tested as substrates of protein tyrosine phosphatase, an important enzyme in cellular signal transduction. The pTyr in bold signifies the tyrosine residue that is phosphorylated. The binding affinities of the polypeptide substrates to the enzyme were found to follow the order: (a) > (c) - (d) >> (b). (a) Asp-Ala-Asp-Glu-pTyr-Leu-lle-Pro-Gln-Gln-Gly (b) Pro-Val-Pro-Glu-pTyr-lle-Asn-Ala-Ser-Val (c) Asp-Ala-Glu-Glu-pTyr-Leu-Val-Pro-Gln-Gln-Gly (d) Asp-Asn-Leu-Tyr-pTyr-Trp-Asp-Glu-Asn-Ser-Ser In addition to the presence of the phosphorylated tyrosine residue, what amino acid a) properties of the polypeptides accounts for the relative order of binding affinities to the enzyme? b) the active site of the phosphatase enzyme that are responsible for the affinity of substrate binding? Assume a pH of 7.4 at the enzyme active site. (Note a phosphatase uses phosphate substrate) What amino acids have side chains that would indicate they are…
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If instead of using 3.5 µM myoglobin (receptor) you used half of this (that is, 1.75 µM myoglobin), what would be that value of the Kd, that you calculated ( how would it change)? Please explain so I can solve on my own :) (How does changing concentration of the receptor in a ligand-receptor binding experiment affect the dissociation constant?)
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bo Consider a uniport system where a carrier protein transports an uncharged substance A across a cell membrane. Suppose that at a certain ratio of [A] inside to [A] outside, the AG for the transport of substance A from outside the cell to the inside, Macmillan Leaming A outside → Ainside, is 10.7 kJ/mol at 25°C. What is the ratio of the concentration of substance A inside the cell to the concentration outside? [A]inside [A]outside Choose the true statement about the transport of A under the conditions described. Because AG is positive, the ratio [A] inside/[A]outside must be less than one. Increasing [A]outside will cause AG for movement of Aoutside to Ainside to become a larger positive number. Movement of Ainside to Aoutside will be spontaneous. Decreasing the concentration of the uniport protein in the membrane will cause AG to become a smaller positive number.
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