Based on the Hill Plot below, this protein-ligand interaction displayslogY1-Y52.50-2.5-2.5nH<10log[L]Uncooperative bindingnH>12.5Binding that obeys the Law of Mass ActionNegative cooperativity5

Hill equation developed by Archibald Hill in 1910 quantitatively describing cooperative ligand…

Answered: Based on the Hill Plot below, this…

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

What is the fractional occupancy of a protein binding site when the ligand concentration (L) =1mM and the ligand equilibrium binding constant at the binding site K10= 10microM. 0.01 B.0.1 C.0.91 D.0.99 none of the listed values
The binding of a ligand quenches the fluorescence of a protein. The following data were acquired: Given that the protein concentration is 0.25 μM, what is the association constant (KA) of the ligand-protein interaction? As this is a rough estimate, you do not need to report uncertainty on your result. The data pic is attached.
12 mM of protein A is combined with 6 mM of ligand X in water. After the protein-ligand complex binding reaches equilibrium, you measure that the free ligand concentration is 3 mM and the concentration of protein-ligand complex is 3 mM. What is the Kd for protein A? Although they would be in mM, do not include units in your answer, only the number as a whole integer.
For the investigation of positive homotropic cooperativity within protein-ligand binding interactions, Hill proposed a reaction as well as a graphic approach. Give the Hill equation as well as a Hill graph and explain the use/meaning of the graph
4.3 Draw a fractional binding curve (θ v.s [L]) for a protein binding to one molecule of L with a Kd of 10 mM.
Amino acids at the interaction site ( F,I and L) and its G protein partner (P, L, Y) are very conserved.If the amino acids are swapped between the protein and GPCR is binding expected to be as tight?
Which is incorrect regarding ligand–protein binding reactions?a. Allosteric modulation of the protein’s binding site occurs directly at the binding site itself.b. Allosteric modulation can alter the affinity of the protein for the ligand.c. Phosphorylation of the protein is an example of covalent modulation.d. If two ligands can bind to the binding site of the protein, competition forbinding will occur.e. Binding reactions are either electrical or hydrophobic in nature
Which of the following situations would produce a Hill plot with nH < 1.0? Explain your reasoning in each case.(a) The protein has multiple subunits, each with a single ligand-binding site. Binding of ligand to one site decreases the binding affinity of other sites for the ligand.(b) The protein is a single polypeptide with two ligand-binding sites, each having a different affinity for the ligand.(c) The protein is a single polypeptide with a single ligand-binding site. As purified, the protein preparation is heterogeneous, containing some protein molecules that are partially denatured and thus have a lower binding affinity for the ligand.
Sketch a plot that shows a typical binding curve for the interactions between a ligand, L (in terms of concentration), and a protein, P.
An antibody binds to another protein with anequilibrium constant, K, of 5 × 109 M–1. When it binds toa second, related protein, it forms three fewer hydrogenbonds, reducing its binding affinity by 11.9 kJ/mole. Whatis the K for its binding to the second protein? (Free-energychange is related to the equilibrium constant by the equa-tion ΔG° = –2.3 RT log K, where R is 8.3 × 10–3 kJ/(mole K)and T is 310 K.)
high and low affinity binding sites require the same amount of ligand to achieve saturation true or false?
In 1965, Monod, Wyman and Changeux put forward the MWC model for cooperative binding of ligands to oligomeric proteins, which also produced the MWC equation above. Give a detailed discussion on this model under the following points:  Hoe die MWC model koöperatiwiteit verklaar. / How the MWC model accounts for cooperative effects.  Wat die effek van allosteriese reguleerders sal wees op die algehele bindingskurwe. / What the effect of allosteric regulators will be on the overall binding curve.  Hoe K-reeks en V-reeks ensieme beïnvloed word deur reguleerders. / How K-series and Vseries enzymes are affected by modifiers.

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

Based on the Hill Plot below, this protein-ligand interaction displays log Y 1-Y 2.5 0 -2.5 -2.5 Uncooperative binding nH<1 0 log[L] OnH>1 Binding that obeys the Law of Mass Action 2.5 Negative cooperativity 5