Provide a simple sketch of the covalentintermediate likely to form between activesite serine residue and diphenylcarbamylchloride. Is DPCC more likely to covalentlybind to serine, aspartate, or histidine?

DPCC: Diphenylcarbamyl chloride has two phenyl group attached to carbamyl chloride. Serine Protease:…

Answered: Provide a simple sketch of the covalent…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 15QP

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Describe the chemical difference between mannose and heptyl alpha-D-mannose. Why does FimH have a higher affinity for heptyl a-D-mannose versus methyl a-D-mannose?
An active site of a hypothetical serine protease with a peptide substrate bound is shown below: This serine protease has 3 specificity pockets (S1, S2, S1') as shown in the figure above. S1 pocket has a glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S1' pocket is deep and hydrophobic. Based on this information you can conclude that R1 is most likely side chain of a. Asp b. Lys c. Lle d. Gly e. Phe
c) A lysine residue in the active site of UstD is involved in forming a covalent Schiff base linkage with the PLP cofactor. In order for this linkage to form, the lysine residue must be in its deprotonated form. Draw the structure of the R group of lysine in this neutral form. What is the ratio of the concentration of this form to that of its conjugate acid form at neutral pH? ( )
Fibrinogen contains tyrosine- O - sulfate. Propose an activated form of sulfate that could react in vivo with the aromatic hydroxyl group of a tyrosine residue in a protein to form tyrosine- O -sulfate.
A peptide with the primary structure Lys-Arg-Pro-Leu-Ile-Asp-Gly-Ala must be synthesized by the methods developed by Merrifield. Calculate the percentage of the peptides synthesized that will be full length and have the correct sequence if the addition of each amino acid residue is 96% efficient. Do the calculation a second time but assume a 99% efficiency for each cycle. full-length peptides with the correct sequence if 96% efficient: full-length peptides with the correct sequence if 99% efficient: % %
Predict the fragments that will be generated from the treatment of the following peptide with: a) trypsin; b) chymotrypsin; c) and S. aureus V8 protease: Gly-Ala-Trp-Arg-Asp-Ala-Lys-Glu-Phe-Gly-Gln
Consider the peptide Asp-Lys-Phe-Glu-Asn-Tyr-Gln-Val-Cys. In a single beaker, you treat this peptide with 2 proteases. One protease cleaves at the N-terminus of aromatic R groups and the other cleaves at the C-terminus of polar, non-ionizable R groups. Following the enzymatic digestion, you want to separate your peptide fragments so that you can identify them. You choose to separate the fragments using an anion exchange column. Beginning at pH=6 you apply your peptide fragments to the column and you gradually decrease the pH of the column stopping the separation when the pH of the column equals 4. Omitting chemical structures, write the amino acid sequence of the peptide fragments that are produced from this digest. Write the order that these fragments will elute from the column (if at all). (Relevant pKa values are: 2.1, 3.8, 4.3, 8.3, 9.6, 10.1, and 10.5)
A tridecapeptide yields the following fragments when partially hydrolized. Determine the sequence of amino acids in the tridecapeptidedrolyzed. Determine the sequence of the tri decapeptide. tridecapeptide à lys-arg + gly-phe-pro + phe-ser-asp-lys + pro-phe-ser + asp-lys-arg-val + gln-ala-tyr + val-trp-gln. Determine the sequence of amino acids in the tridecapeptide
Given the undecapeptide un sequenced Ala2, Arg, Glu, Lys, Met, Phe, Ser, Thr, Trp, Val. Edman Degradation identified Ala. It is further analyzed and degraded to four fragments using trypsin- catalyzed hydrolysis and yielded the following Ala – Glu – Arg ;Thr – Phe – Lys ; Lys ; and Met – Ser – Trp – Val . To further analyze the undecapeptide A.A Sequence, Chymotrypsin -catalyzed hydrolysis identified two fragments Ala – Arg – Glu – Phe – Thr and Lys – Met – Ser – Trp – Val and lastly treatment with cyanogen bromide identified two fragments: Ala – Arg – Glu – Lys – Met – Phe – Thr – Val; and Trp – Ser what is the name of the undecapeptide?
A heptapeptide was found to have an amino acid composition of Asp, Leu, Lys, 2 Met, Phe and Tyr. (a) Trypsin has no effect on the heptapeptide. (b) The phenyl thiohydantoin released by Edman degradation revealed phenylalanine in the N-terminus. (c) Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys, and Met. (d) Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free Lys. What is the amino acid sequence of this heptapeptide? Answer Format: (Three letter abbreviation with dash ie., Ala-Gly-…) *
Some of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.
In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys-The hydrophobic residues in this sequence are presented in boldface type.Suggest a possible reason for the periodicity in their spacing.

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