affinity of a protein-protein or protein-ligand interaction can be described by theDissociation Constant, Kd (written below). Consider a protein P and its inhibitor,I.I inhibits P's activity when bound to it:koff _ [A][B]Dissociation Constant: Ka=koN[AB]QuestionWhen [I] is 10-7 M, 99% of P's activity is inhibited. What is the Kd of this Protein-Inhibitor interaction?

Protein can function as enzymes, signal molecule, ligand, receptor, etc. Its function can be…

Answered: When [I] is 10-7 M, 99% of P's activity…

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

See similar textbooks

Similar questions

For the following problem, indicate whether enzyme is repressed (-) or produced (+). Please show all possible outcomes.
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?)
You are studying how your Lys-Val-Thr tripep de interacts with another pep de, which places an Asp in close proximity to the Lys on your pep de. How would the presence of an Asp side chain affect the pKa of the Lys side chain? Briefly explain your reasoning. (remember pKas are rela ve, pKa=log([H+][A-]/[HA])
Two proteins, A and B, bind to the same ligand, L, with the binding curvesshown below. What is the dissociation constant, Kd , for each protein? Which protein (A or B) has a greater affinity for ligand L?
The affinity of hemagglutinin for sialic acid is quite low, with a Kd of approximately 5 mM. How does efficient attachment occur with such a low-affinity interaction?
help
Why might a compound resembling ADP function as an inhibitor of a protein kinase?
Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…
What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine? In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?
Consider, for example, that a particular serine residue is phosphorylated to activate the protein. In the lab, a similar effect is achieved by mutating this residue to either a D (aspartic acid) or E (glutamic acid). What could be the reason?
For the conversion of Trypsinogen into Trypsin, Write the total number of amino acids should be cleaved and from which site?
Why would the amount of protein E bound to immobilized heparin fall in the presence of soluble heparin?

SEE MORE QUESTIONS

Recommended textbooks for you

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

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

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

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

SEE MORE TEXTBOOKS

When [I] is 10-7 M, 99% of P's activity is inhibited. What is the Kd of this Protein- Inhibitor interaction?