5.. A sample of cells has a total receptor concentration of 25 mM. Ninety percent of thereceptors have bound ligand and the concentration of free ligand is 125 µM. Calculate the Kfor the receptor ligand interaction. (a) What is the AG° for binding for this interaction at 25°C?

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Answered: 5.. A sample of cells has a total…

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter6: Cell Communication

Section6.3: Reception

Problem 4LO

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22
Estimate the binding affi nity of a ligand for its receptor from the followingdata:
From the Hill Plot below, the of the first binding event for the receptor-ligand system under study is: Q1 4nM Ο 10 μΜ -2 nM 2 nM Calculate the Hill Coefficient from the receptor-ligand binding data below: Q2 4 100 2 3 (0-1) 60 log 10 8 6 4 2 0 -2 -4 -6 -6 -4 -2 0 2 4 log [L] (nM) 6 8 10
2) After plotting actin bound to cofilin versus the cofilin concentration, you generate the figure below. v (cofilin binding density) 1 0.8 0.6 0.4 0.2 0 2 4 6 8 [S. pombe cofilin] free (UM) 10 a) What is the Kd you measure for this interaction? b) What is the AG of the interaction? c) Based on the data, is there anything you suspect about the binding of protein and ligand?
3) You are investigating the ionic selectivity of an ion channel opened by activation of a specific group of ionotropic receptors. You use the ionic concentrations shown in the following table and determine that the reversal potential for activation of the receptors is -10 mV? Ion Intracellular (mM) Extracellular (mM) Equilibrium Potential (E1on) K+ 140 5 Na+ 10 145 Ca2+ 0.0001 2 Cl- 6. 106 a) Use the Nernst equation to calculate the equilibrium potential for each ion above. b) Is it likely that ion channel is selective to a single ion? Why or why not? c) Provide one possible ionic selectivity for this channel that could give rise to the following reversal potential. d) How would you determine if this possibility is correct?
27.
In a Myoglobin and azide ligand-receptor binding experiment, instead of using 3.5 µM myoglobin you used half of this (1.75 µM myoglobin), what would be that value of the Kd, that you calculated (how would the Kd change)?
7. Given the following concentrations: K* ICF 140 mM Na CH 12 mM 12 mM ECF 3 mM 145 mM 120 mM a) Calculate the equilibrium potentials of K, Na* and Cl using the Nernst equation. EK = ENa = ECi = b) In the case above, if the membrane is permeable only to K, what would be the predicted membrane potential? c) If the membrane is equally permeable to K and Na", and impermeable to all other ions, what would be the predicted membrane potential?
The top panel (a) of this figure shows the graded potential change (far right, upper, electrical trace) that results from ligand binding to the ligand gated Na+ channel. The bottom panel of this figure (b) shows a graded potential change (far right, lower, electrical trace) that results from ligand binding to a ligand gated Cl- channel. From this trace you know (Vm = -70 mV) 1. ECl- is -70 mV 2. ECl- is more negative than -70 mV (i.e., -80 mV) 3. ECl- is more positive than -70 mV (i.e., -60 mV)
In the two competition study experiments below, what can you say about the relative affinities of the labeled ligand and the unlabeled competitor ligand? Remember to check the concentrations of both in each experiment. extracellular plasma membrane intracellular Competition study Competitor unlabeled ligand Labeled ligand †††† Receptor 10 nM Competitor unlabeled ligand 10 nM Labeled ligand ŸŸŸŸ 9 nM Competitor unlabeled ligand 3 nM Labeled ligand
α-Bungarotoxin is a powerful neurotoxin found in the venom of a poisonous snake (Bungarus multicinctus). It binds with high specificity to the acetylcholine receptor (AChR; an integral membrane protein) andprevents its ion channel from opening. This interaction was used to purify AChR from the electric organ of torpedo fish.(a) Outline a strategy for using α-bungarotoxin covalently bound to chromatography beads to purify the AChR protein. (b) Outline a strategy for the use of [125I]α-bungarotoxin to purify the AChR protein.
The Graph below shows the binding curves of two proteins (A and B) for the same ligand (L). Use this Graph and determine the dissociation constant, K, for both proteins. Which protein (A or B) has a greater affinity for ligand L? Which of the two proteins would be more easily inhibited by an antagonist? 1.0 Y 0.5 2 A 4 6 B 8 [L] (μM) 10 12 14 16

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5.. A sample of cells has a total receptor concentration of 25 mM. Ninety percent of the receptors have bound ligand and the concentration of free ligand is 125 µM. Calculate the Kp for the receptor ligand interaction. (a) What is the AGº for binding for this interaction at 25°C?