A (non-allosteric) protein binds its ligand with a Kd of 2.5 mM. What proportion of the...
A (non-allosteric) protein binds its ligand with a Kd of 2.5 mM. What proportion of the ligand-binding sites will be occupied at a protein concentration of 1.0 mM and a ligand concentration of 1.5 mM?
The answer is 37.5%, but how do you find this answer?
Homework Answers
![conce [l] = ligand concentration O = fraction of protein occupies 1. ligand binding site - O= [L] [L]+ ka I.SALM 1.5mm + 2.5m](http://img.homeworklib.com/questions/89c96b40-e567-11eb-b038-49216679ca47.png?x-oss-process=image/resize,w_560)
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A (non-allosteric) protein binds its ligand with a Kd of 2.5 mM.
What proportion of the...
A binding protein binds to a ligand with Kd=30nm. What is the concentration of ligand when...
A binding protein binds to a ligand with Kd=30nm. What is the
concentration of ligand when the [L] when the fraction
bound,,
is a) 0.25, b) 0.6 and c) 0.95.
(2) In isolation, a DNA-binding protein binds to its regulatory sequence with a Kd of 1.0 M. Another DNA binding protein binds to another sequence on the same DNA a few bases away with a Kd of 5....
(2) In isolation, a DNA-binding protein binds to its regulatory sequence with a Kd of 1.0 M. Another DNA binding protein binds to another sequence on the same DNA a few bases away with a Kd of 5.0 HM when alone. The two proteins each have a domain which binds to the other with an interaction energy of -2.7 kcal/mole: (a) Draw the thermodynamic box which represents all four states of this system (b) what are the affinities for each...
Two proteins bind to the same ligand, and protein A has a fractional saturation of 0.5...
Two proteins bind to the same ligand, and protein A has a fractional saturation of 0.5 when the ligand concentration is 0.5 mM, while protein B has a fractional saturation of 0.25 at 0.3 mM of the ligand. Which protein binds the ligand more strongly, and what is the dissociation constant for that protein-ligand interaction? *** I know the answer I just need the steps to do it*** Answer: Protein A binds more strongly, and Kd = 0.5 mM.
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...
A binding protein binds to a ligand L with a K_d of 400 nM. What is...
A binding protein binds to a ligand L with a K_d of 400 nM. What is the concentration of ligand when is a) 0.25, b) 0.6, c) 0.95?
1. What does it mean to have positive cooperatively in protein-ligand binding? 2. The protein “Mariota”...
1. What does it mean to have positive cooperatively in protein-ligand binding? 2. The protein “Mariota” binds to the ligand “football” with an association rate of 8.0 x 10 103M-1s-1 and an overall dissociation constant, Kd of 10 nM. Calculate the dissociation rate, kd, including appropriate units. 3. An antibody binds to an antigen with a Kd of 8 X 10-6M. At what concentration of antigen will the fractional saturation (Υantigen) be (a) 0.2, (b) 0.5, (c) 0.6, and (d)...
41. Which of the following statements about protein-ligand binding is correct? A) The K is equal...
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...
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...
You have ligand that you know binds to your receptor, since you’ve measured its affinity using...
You have ligand that you know binds to your receptor, since you’ve measured its affinity using isothermal titration calorimetry. You want to know the exact pose of the ligand in its binding pocket, so you use a computer simulation to dock it to the receptor structure. Surprisingly, your software shows the ligand on the protein surface, not in the pocket at all. What type of experiment could you do to confirm the location of the binding site and pose of...
Protein A Protein B [PL), UM 0.00 0 0.000 0 1) (10 marks) You study ligand...
Protein A Protein B [PL), UM 0.00 0 0.000 0 1) (10 marks) You study ligand binding to two proteins, A and B. You measured the concentration, (PL), of the ligand-bound form of the protein at various ligand concentrations, [L]. The data are summarized in the two tables below. Note that you do not know the total concentration of the protein, but you know that adding more ligand did not noticeably change the bound- protein concentration. [L), UM [PL], uM...
A binding protein binds to a ligand with Kd=30nm. What is the
concentration of ligand when the [L] when the fraction
bound,,
is a) 0.25, b) 0.6 and c) 0.95.
(2) In isolation, a DNA-binding protein binds to its regulatory sequence with a Kd of 1.0 M. Another DNA binding protein binds to another sequence on the same DNA a few bases away with a Kd of 5.0 HM when alone. The two proteins each have a domain which binds to the other with an interaction energy of -2.7 kcal/mole: (a) Draw the thermodynamic box which represents all four states of this system (b) what are the affinities for each...
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...
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...
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...
Protein A Protein B [PL), UM 0.00 0 0.000 0 1) (10 marks) You study ligand binding to two proteins, A and B. You measured the concentration, (PL), of the ligand-bound form of the protein at various ligand concentrations, [L]. The data are summarized in the two tables below. Note that you do not know the total concentration of the protein, but you know that adding more ligand did not noticeably change the bound- protein concentration. [L), UM [PL], uM...
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