The structure of a peptide is shown below:OHHNNH,How many hydrolytic products will be obtained by cleavage withtrypsin, a protease?А. 2В. 3О С.4O D. 5E. none; trypsin will not cleave the peptide

Peptides of proteins are composed of 20 standard amino acids attached together via peptide bonds.…

Answered: The structure of a peptide is showwn…

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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Similar questions

You have a solution with the mixture of the following peptides: 1) Wing-Cys-Gly 2)phe-tyr-trp-phe 3)glu-asp-glu-ileHow are each of them charged at the following pH?a) 3 b) 5 c) 7 d) 9
Draw the structure of the following: (in the image provided)Use the amino acids below.F - PhenylalanineI - IsoleucineG - GlycineH - HistidineT - ThreonineE - Glutamic acidR - Arginine
Name another condition besides heat and exposure to a bond disruptor (like alcohol) that could affect the ability of a protein to maintain its shape. Explain.
Write the structure, identify the groups and describe the chemical properties of these amino acids. A. alanine B. Serine C. Leucine D. Phenylalanine E. Tryptophan
Draw the titration curves for the following AA’s: Aspartic acid, Alanine, Lysine, Valine, Serine, and Trrosine.
Examine the following peptide and the inserted table, and answer the 2 questions below: Thr-Glu-Pro-Ile-Val-Ala-Pro-Met-Glu-Tyr-Gly-Lys 1. Estimate the net charge of the peptide at pH 2.0. Explain. 2. Estimate the net charge of the peptide at pH 7.0. Explain.
You have isolated from a rare fungus an octapeptide that prevents baldness and you wish to determine its amino acid sequence. The amino acid composition is K2, D, Y, F, G, S, A. Reaction of the intact peptide with dansyl chloride yields dansyl-A. Cleavage with trypsin yields peptides whose compositions are: (K, A, S) and (G, F, K) plus a dipeptide. Reaction with chymotrypsin releases free D, a tetrapeptide with composition (k, S, F, A) and a tripeptide whose composition following acid hydrolysis is (G, K, Y). The enzymatic digests are each carried out on the whole, undansylated peptide.What is the sequence?
What are the charges of the following amino acids peptides at ph 14? 1. GLAVV 2. RRKKQ
Which of the following is the C-terminal amino acid in the polypeptide glycyl-alanyl-leucyl-valyl-glutamine? A. Glycine B. Alanine C. Leucine D. Valine E. Glutamine
Name another condition besides heat and exposure to a bond disruptor (like alcohol) that could affect the ability of a protein to maintain its shape.
Which of the following amino acids is most likely to be found on the outside of a soluble protein, and which of them is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acidside chain in each case and that the protein is folded up into its globular form.)(a) Valine (b) Aspartate(c) Histidine (d) Alanine
What protecting groups in solid-phase peptide synthesis NOT do? a)Activate the carboxlic acid to have a good leaving group b)Prevent the amino acid backbones from randomly polymerizing in solution c)Prevent the amino acid side chains from undergoing uncontrolled chemistry d)Get cleaved from the peptide when the peptide is cleaved from the resin

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The structure of a peptide is showwn bélöw: NH, HN