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Short answer questions: 21. Protein A has a binding site for ligand L with a Ka...
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 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.
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...
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...
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)...
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.
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
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.
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...
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...