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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Which of the following statements is true O Sphingomyelin posses phosphoryl serine in addition to two long hydrocarbon chains, one contributed by a fatty acid and the other by sphingosine OLipid compositions of membrane mono-layers are symmetrical O Unsaturated fatty acids have double bond(s) in the cis configuration In ABO blood typing, lack of glycosyltransferase and galactosyltransferase produces AB blood group
You have synthesized an oligopeptide containing an RGD motif surrounded by other amino acids. What is the effect of this peptide when added to a fibroblast cell culture grown on a layer of fibronectin adsorbed to the tissue culture dish? Why does this happen?
A mutation of Lysine 82 (in the DPG-binding pocket) to Arginine in beta sub-unit will most likely result in Not enough information Higher than normal binding affinity to oxygen Lower than normal binding affinity to oxygen Normal binding to oxygen
What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine? In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?
The G-protein Ras is involved in proliferative signaling, and is mutated is a large fraction of human cancers. Almost all mutations in Ras mutate the glycine at codon 12. These mutations lock Ras in an active conformation. How will the GTPase activity of a Ras protein with a G12 mutation compare to a normal Ras protein without the mutation? (10 words maximum)
Why is salbutamol better than isoproterenol in asthma management in terms of their binding sites?
Please help with complete answers of both the parts
Identify a protein that can contain a temperature-sensitive mutation that would explain these observations O Atvtoptesme protein that is unabte to bind to IMP aarc OAlgn unction protein tut hindh tightly to IMP 3C Acelt corte protein that unuble tu bind to IMP37C OAtnnsmemtrrane proten that binds tighely to Mat 37C O An entracelr matrie pootein that bt tightly 1o İMPat 37C
14
A3 KcsA K+ ion channel has their selectivity filer arranged as amino acid "TVGYG", so it can only binding with K+ ion, if this amino acid arrangement changed to "TVGDG", it can also select Na+ ion. why?
A biotech company develops a biosensor that measures the presence of proteins activated by growth factor signaling cascades. Which binding domain would you use to each of the following activation peptides or signaling molecules. Phosphotyrosine A. SH2 Domain A peptide with the sequence Arg-Ala-Pro-Pro-Leu- B. Bromodomain Pro C. 14-3-3 Domain ◆ Phosphatidyl inositol Triphosphate (PIP3) Phosphoserine Acetylated Lysine D.PH Domain E. SH3 Domain
1. The CFTR protein is a chloride channel in the cell membrane. Use your understanding of the biochemical properties/categories of amino acids and how they interact with membrane phospholipids to predict the distribution of charged/polar, and non-polar amino acids within the domains of CFTR listed below. Consider one category to include the charged amino acids and the polar amino acids and the other category to include the non-polar amino acids. For each domain, predict which category of amino acids is likely to be most abundant. Also, explain the rationale behind your prediction. Protein domain Prediction (Charged/Polar or Non-Polar amino acids?) Explanation for prediction TMD1 and TMD2 (transmembrane domains, parts 1-12) ECLs and ICLs (extracellular and intracellular loops) NBD1 and NBD2 R

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