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- Give one biological molecule and discuss briefly the intermolecular forces of attraction involvedWhich of the following must be true based on the data below for ligand L binding to protein A and to protein B? Choice 1 of 4:Protein A binds at least 2 molecules of ligand L. Choice 2 of 4:The Kd for ligand binding to B is approximately 4 micromolar. Choice 3 of 4:When exposed to ligand L, protein A reaches maximal binding faster than does protein B. Choice 4 of 4:Protein B must adopt at least 2 different conformations with different binding affinities.For a protein that binds multiple ligands with negative cooperativity, which of the following is true? Each ligand bound increases the dissociation constant for subsequent ligands. Ligands cannot bind to the protein. The dissociation constant is not affected by binding of other ligands. Each ligand bound decreases the dissociation constant for subsequent ligands.
- Which allosteric model can explain negative cooperativity?For each of the following pairs of amino acids, identify the strongest type of intermolecular forces involved when the side chains interact. Explain in terms of the chemical structures of the amino acid side chains. Use the following list: disulfide bridge, hydrogen bonding, hydrophobic interaction, or salt bridge. a) D and H b) C and C c) L and A d) G and S e) N and TWhich noncovalent interactions (discussed in Section 8.2) are responsible for the cohesion of lipid molecules? Is the overall strength of these forces weak or strong? Why are lipids incompatible with water?
- A synthetic immunoglobulin (Protein X) was created by a scientist to recognize retroviruses. However, Protein X became inactive upon subjection to sodium dodecyl sulfate, a detergent. Which of the following molecular forces of attraction is not disrupted by the detergent? Dipole dipole interaction Covalent interaction H-bonding Hydrophobic interactionProtein A binds to Ligand X with a Kd of 1 μM. Protein B binds to Ligand Y with a Kd of 100 nM. Which of the following statements is TRUE? A. Protein A binds Ligand X ten times tighter than Protein B binds Ligand Y B. At a sufficiently high concentration of ligand, the binding becomes irreversible C. When the concentration of Ligand X is 1 μM, 50% of Protein A is bound to ligand D. Protein B binds to Ligand Y with a Kd of 1 × 10-8 mol/L. E. When both binding reactions are at equilibrium, Protein A has more Ligand X bound than Protein B has ligand Y bound The answer is C, could you show how to get the answer? ThanksWhat type(hydrophilic, hydrophobic, acid, base) side chains might be attracted to each other? What type(hydrophilic, hydrophobic, acid, base) side chains might repel each other?
- 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 16Which are the Three binding sites with the same chemical specificity but different affinities for a ligand?Sketch a plot that shows a typical binding curve for the interactions between a ligand, L (in terms of concentration), and a protein, P.