Below is an image of a calcium binding site on the calmodulin protein.What statement is correct regarding this Ca2+ binding?140ASN 136GLIL29131GL 132133Time left 1:1O a. deprotonated acidic side chains are important for Ca2+ bindingO b. Ca2+ binding usually does not result in conformational changes in a proteinO c. deprotonated basic residues are important for Ca2+ bindingO d. Ca2+ binding to proteins is usually done by coordination with one side chain

Calmodulin is a calcium-binding protein whose activity is regulated by calcium ions.Calcium binds to…

Answered: Below is an image of a calcium binding…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Look at the figure and predict what would happen if the SRPRNA was unable to stimulate the GTPase activities of the GTPbindingproteins within SRP and the SRP receptor.
The bioactive conformation of lead compound I was confirmed when a crystal structure was r. obtained showing I bound to its target (an enzyme). Ala-312 in His-42 Val-307 CI Asp-305 Phe-47 H. Ser-254 I bound to target protein Using the information shown above, draw the structure of an analog that you predict will exhibit improved binding to the target. Explain how you arrived at this proposed analog structure.
Which peptide in below pair has side chains that exhibit predominantly van der Waals forces? Tyr–Asp–Leu–Lys–His or Phe–Asn–Leu–Leu–Met
A binding curve for the binding of the amino acid tryptophan to the protein called TxtE is shown below. Estimate the association equilibrium constant (Ka; in units of M-1) for Trp binding to TxtE.
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What molecule allowed our target protein to elute off our affinity column? O a. lysozyme O b. BSA O c. imidazole O d. Laemmli O e. PMSF What information can isoelectric focusing provide about a protein? choose one or more: a. its pl b. its degree of purity c. its Km d. its molecular weight
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9. Shown below is a binding pocket for a protein with a ligand bound. The ligand interacts with a serine and a valine side chain. ligand a. Briefly explain, in terms of Ka, the effect of a mutation that replaces the serine residue with a valine residue. b. Briefly explain, in terms of Kd, the effect of a mutation that alters the ligand (as seen below) binding to the original, unmutated, binding site. :0: ligand 2

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