Ligand L binds to a binding protein with a Ka of 400 nM. Calculate the ligand concentration based on the fraction of bindingsites occupied by the ligand (Y). Express each answer to two significant figures.Calculate the ligand concentration when Y is 0.25.[L] =µMCalculate the ligand concentration when Y is 0.60.[L] =µMCalculate the ligand concentration when Y is 0.95.[L]µM

Ligands are type of Lewis bases which has the capacity to donate a pair of electrons and form a…

Answered: Ligand L binds to a binding protein…

Principles of Instrumental Analysis

7th Edition

ISBN:9781305577213

Author:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Publisher:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Chapter14: Applications Of Ultraviolet-visible Molecular Absorption Spectrometry

Section: Chapter Questions

Problem 14.19QAP

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A protein binds a ligand with a ka value of 7.4 x 104 M-1s-1 and a kd value of 6.4 x 10-4 s-1. What is the KD value of this binding event in units of nM? Please report your answer to two significant figures and include units.
Relationship between Affinity and Association & Dissociation Constant. Four proteins (A-D) all bind the same ligand (X), with different affinities. For protein A & B we know that they have a binding site for X with a Kd (dissociation constant) of 10-5and 10-8M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 103and 105M, respectively. Which protein has the highest affinity for ligand X? Explain your reasoning.
I did not understand soultion for the question.. The relationship between Affinity and Association & Dissociation Constant. Four proteins (A-D) all bind the same ligand (X), with different affinities. For protein A & B we know that they have a binding site for X with a Kd (dissociation constant) of 10⁻⁵and 10⁻⁸ M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 10³and 10⁵M, respectively. Which protein has the highest affinity for ligand ? Explain your reasoning. How do you make them all in same constant so that values can be compared and the one with highest Ka or lowest Kd (Highest affinity in both cases) can be ruled out.
A protein binds a ligand with a KD value of 0.25 M. If you are at a ligand concentration of 0.63 M, what is the fraction bound? Please report your answer to two significant figures. There should be no units in your answer
A dimeric binding protein has a KD1 of 50 nM and a Hill coefficient of 1.4. What is the fraction of the protein that has ligand bound at 17 nM concentration of ligand?
Molar absorptivities of Nickel and Cobalt with 8-quinilinol are εCo = 3529 and εNi = 3228 at 365 nm, and εCo = 428.9 and εNi = 0 at 700 nm. Calculate concentration of nickel and cobalt in solution that gave Abs = 0.617 at 365 nm and Abs = 0.0235 at 700 nm
The molar absorptivity (ε) of the FeSCN2+ complex ion is 4700 M-1 · cm-1 at a wavelength of 450 nm. Using a 1-cm sample tube, you measure the absorbance as (2.0x10-1). What is the concentration of FeSCN2+? What is your answer? _____________x10^_____
If the association constant, Ka, for a certain protein-ligand pair is 50,000, what is the dissociation constant, Kd? Please provide your answer in decimal form, not scientific notation.
Molar absorptivity data for the cobalt and nickel complexes with 2,3-quinoxalinedithiol are εCo = 36400 and εNi = 5520 at 510 nm and εCo = 1240 and ε Ni = 17500 at 656 nm. A 0.361-g sample was dissolved and diluted to 150.0 mL. A 25.0-mL aliquot was treated to eliminate interferences; after addition of 2,3-quinoxalinedithiol, the volume was adjusted to 50.0 mL. This solution had an absorbance of 1.037 at 510 nm and 0.422 at 656 nm in a 1.00-cm cell. Calculate the concentration of cobalt (in ppm) in the initial solution prepared by dissolving the sample.
Molar absorptivity data for the cobalt and nickel complexes with 2,3-quinoxalinedithiol are εCo = 36400 and εNi = 5520 at 510 nm and εCo = 1240 and ε Ni = 17500 at 656 nm. A 0.361-g sample was dissolved and diluted to 150.0 mL. A 25.0-mL aliquot was treated to eliminate interferences; after addition of 2,3-quinoxalinedithiol, the volume was adjusted to 50.0 mL. This solution had an absorbance of 1.037 at 510 nm and 0.422 at 656 nm in a 1.00-cm cell. Calculate the concentration of cobalt (in ppm) in the initial solution prepared by dissolving the sample. Calculate the concentration of nickel (in ppm) in the initial solution prepared by dissolving the sample.
Molar absorptivity data for the cobalt and nickel complexes with 2,3-quinoxalinedithiol are εCo = 36400 and εNi = 5520 at 510 nm and εCo = 1240 and ε Ni = 17500 at 656 nm. A 0.361-g sample was dissolved and diluted to 150.0 mL. A 25.0-mL aliquot was treated to eliminate interferences; after addition of 2,3-quinoxalinedithiol, the volume was adjusted to 50.0 mL. This solution had an absorbance of 1.037 at 510 nm and 0.422 at 656 nm in a 1.00-cm cell. Calculate the concentration of cobalt (in ppm) in the initial solution prepared by dissolving the sample. Calculate the concentration of nickel (in ppm) in the initial solution prepared by dissolving the sample. I've asked this question multiple times and still have not gotten the right answer. This is my last question and I don't know what to do if this is also wrong.
Molar absorptivities of Nickel and Cobalt with 8-quinilinol are εCo = 3529 and εNi = 3228 at 365 nm, and εCo = 428.9 and εNi = 0 at 700 nm. calculate concentration of nickel and cobalt in solution that gave Abs=0.617 at 365nm and Abs=0.0235 at 700nm.

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