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?
A binding protein binds to a ligand L with a K_d of 400 nM. What is...
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.
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...
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)...
In E. coli, maltose-binding protein binds maltose in the periplasm to deliver the sugar to a maltose ABC transporter. Maltose-binding protein is a simple monomeric protein. It is 20% saturated when the maltose concentration is 300 nM. What is the Ko of maltose-binding protein for its ligand? A. 300 nM B. 600 nM C. 900 nM D. 1200 nM E. 1500 nM
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...
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?
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...
1. The Hill Equation a) Derive the Hill Equation for a protein binding a single ligand (i.e. the reaction P + PL) and explain how a plot will appear. Derive the Hill Equation for a dimeric protein that simultaneously binds two ligands (i.e. the reaction: P2 2L- P2L2) and explain how a plot will appear. Explain what is problematic about the reaction shown in question b) L b) c) 1. The Hill Equation a) Derive the Hill Equation for a...
. For a protein P binding to a ligand L, derive the Scatchard equation that relates the inverse of the concentration of the bound form (1/[P:L]) to the inverse of the concentration of free form (1/[P]).
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.