Assume that the concentration of the ligand is much greater than the concentration of the protein. When ligand Y is pres...
Assume that the concentration of the ligand is much greater than the concentration of the protein. When ligand Y is present at a concentration of 2 x 10-6 M, 50% of the binding sites on the molecules of protein X are found to be occupied. If the concentration of the ligand is increased to 3 x 10-6 M, what fraction of the binding sites will be occupied?
Please explain the steps to solve this problem.
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![Fractional Constant (0) = [1] [2] tko [2] - Concentration of free ligand ko - Dissociation constant In first case TL = 2 x 10](http://img.homeworklib.com/questions/041455c0-0145-11ea-bfd5-b9e81ff5b22f.png?x-oss-process=image/resize,w_560)
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Assume that the concentration of the ligand is much greater than the concentration of the protein. When ligand Y is pres...
Wrine a rate equation depicting the rate of change in the concentration of the protein ligand...
Wrine a rate equation depicting the rate of change in the concentration of the protein ligand eomples formedi acvonding to the reaction below e5 pts ndng Se LP L+P k Protein (P) Protein (P) The reaction above has a 2 onder association rate constant (k.) of 500 mM's and a 1" order dissociation rate constant (ka) of 10 s, What are the equilibrium association (KA) and dissociation (Kn) constants for this basic ligand binding event (I BP) 2.) Use the...
LLI (nM) 92 The data at right describe the binding of a ligand to a protein:...
LLI (nM) 92 The data at right describe the binding of a ligand to a protein: 0.1 0.07 s [L] is the concentration of free ligand. e is the fraction of sites on the protein that are occupied by the ligand. (Note that some textbooks use terms like v or Y, instead of 6, to denote fractional saturation) 0.4 0.23 0.36 Answer parts (a) and (b) below. 0.55 1.2 (a) Which of the following graphs could be used to estimate...
Short answer questions: 21. Protein A has a binding site for ligand L with a Ka...
Short answer questions: 21. Protein A has a binding site for ligand L with a Ka of 10-6 M. Protein B has a binding site for ligand L with a Ka of 10'M. (a). Which protein has a higher affinity for ligand L? Explain your reasoning. (b). At what concentration of ligand L is proteins A half-saturated. At what concentration of L is protein B half-saturated. [L] y = [L] + Ka 22. A protein binds to a ligand L...
Usually a protein-binding curve is a hyperbolic function, with theta on the y-axis and [total ligand]...
Usually a protein-binding curve
is a hyperbolic function, with theta on the y-axis and [total
ligand] on the x-axis. We can only assume that [Free L]=[L total]
when the ligand is in excess of the protein. For example the
[protein] would be 0.001 nM and you start adding ligand in .05nm
increments. But what would the binding curve above look like if the
[receptor]=1 nM: the ligand concentration is no longer in excess of
the protein concentration? Would you still...
41. Which of the following statements about protein-ligand binding is correct? A) The K is equal...
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Scatchard analysis may give information about? O A. the ligand binding constant (Kb) of a protein,...
Scatchard analysis may give information about? O A. the ligand binding constant (Kb) of a protein, OB. the number of ligand binding sites on a protein, the type of homotropic cooperativity with ligand binding, OD. Bmax: O E. all of the above, OF. none of the above. In glycolysis, fructose 1,6-bisphosphate is converted to two products with a AG'ยบ of 23.8 kJ/mol. Under what conditions encountered in a normal cell will the free-energy change (AG) be negative, enabling the reaction...
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Please help! Ligand X forms a complex with both cobalt and copper, cach of which has...
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Ligand X forms a complex with both cobalt and copper, cach of which has a maximum absorbance at 510 nm and 645 nm, respectively. A 0.217 g sample containing cobalt and copper was dissolved and diluted to a volume of 100.0 mL. A solution containing ligand X was added to a 50.0 mL aliquot of the sample solution and diluted to a final volume of 100.0 mL. The measured absorbance of the unknown solution was 0.493 at 510...
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Wrine a rate equation depicting the rate of change in the concentration of the protein ligand eomples formedi acvonding to the reaction below e5 pts ndng Se LP L+P k Protein (P) Protein (P) The reaction above has a 2 onder association rate constant (k.) of 500 mM's and a 1" order dissociation rate constant (ka) of 10 s, What are the equilibrium association (KA) and dissociation (Kn) constants for this basic ligand binding event (I BP) 2.) Use the...
LLI (nM) 92 The data at right describe the binding of a ligand to a protein: 0.1 0.07 s [L] is the concentration of free ligand. e is the fraction of sites on the protein that are occupied by the ligand. (Note that some textbooks use terms like v or Y, instead of 6, to denote fractional saturation) 0.4 0.23 0.36 Answer parts (a) and (b) below. 0.55 1.2 (a) Which of the following graphs could be used to estimate...
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Usually a protein-binding curve
is a hyperbolic function, with theta on the y-axis and [total
ligand] on the x-axis. We can only assume that [Free L]=[L total]
when the ligand is in excess of the protein. For example the
[protein] would be 0.001 nM and you start adding ligand in .05nm
increments. But what would the binding curve above look like if the
[receptor]=1 nM: the ligand concentration is no longer in excess of
the protein concentration? Would you still...
41. Which of the following statements about protein-ligand binding is correct? A) The K is equal to the concentration of ligand when all of the binding sites are occupied. B) The K is independent of such conditions as salt concentration and pH. C) The larger the K. (association constant), the weaker the affinity. D) The larger the K. the faster is the binding. E) The larger the K, the smaller the K. (dissociation constant) 42. The ability of O, to...
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Please help!
Ligand X forms a complex with both cobalt and copper, cach of which has a maximum absorbance at 510 nm and 645 nm, respectively. A 0.217 g sample containing cobalt and copper was dissolved and diluted to a volume of 100.0 mL. A solution containing ligand X was added to a 50.0 mL aliquot of the sample solution and diluted to a final volume of 100.0 mL. The measured absorbance of the unknown solution was 0.493 at 510...
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32. Study the signaling pathway illustrated below, which involves two different receptors. Assume that a protein is active only when it is activated, but not inhibited, by its upstream signaling molecules. Activation and inhibition are indicated by normal and blunt arrows, respectively. Assume that the transcription regulator can be activated by either the binding protein or the kinase that are immediately upstream of the transcription factor. Under which of the following conditions will the expression of target:gene "X" be induced?...
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