5. A peptide was cleaved into two smaller peptides with cyanogen bromide (CNBI) and into twodifferent peptides by trypsin (Tryp). Their sequences were as follows:CNB 1: Gly-Thr-Lys-Ala-GluCNBR 2: Ser-MetTryp 1: Ser-Met-Gly-Thr-LysTryp 2: Ala-GluWhat was the sequence of the original peptide?

The given peptide sequences are: CNBr 1: Gly-Thr-Lys-Ala-Glu CNBr 2: Ser-Met Tryp 1:…

Answered: A peptide was cleaved into two smaller…

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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you have the following peptide Arg-Ile-Pro-Leu-Asp-Lys-Glu The net charge on this peptide at pH 7.0 is ?. The net charge on this peptide at 1M HCl is ?.
The structure below shows that of a polypeptide composed of multiple amino acid residues, some of which have undergone post-translational modifications in their side chains. HN- NH2 NH residues. 1) This polypeptide has 2) Using one-letter abbreviations, the sequence of the polypeptide (before post-translational modification) is
A peptide containing 18 amino acid residues in its sequence was partially hydrolyzed and peptides A–D were detected in the resulting mixture. Draw the sequence of the original peptide.A Phe-Gly-AlaB Ser-Ser-Ser-Trp-Phe-Gly-AlaC Phe-Phe-Met-Ala-Ala-Pro-Trp-CysD Met-Ala-Ala-Pro-Trp-Cys-Leu-Ile-Leu-Ser-Ser
Why is the pKa of the arginine side chain greater than the pKa of the lysine side chain?
42
Given the following diagram of how protein AWESOME1 binds to it's target DNA, describe the potential effects of each of the 5 mutations shown below. The wild-type sequence of a helix #1 is also shown in the blue box, and all the mutations are in helix #1 (see numbers for identifying particular residues). a helix #1 R(1)-V-I-L-Y-F-W-I-M-Y-F-S-H-Y-W-R(16) #1 Predict the consequence of the following mutations: 1) Arg(1) to Glu 2) Arg(1) to Ala 3) Phe(6) to lle 4) Trp(7) to Phe 5) Met(9) to Pro in
identify the interaction that may be produced between the side chain of amino acid residues found at the N-terminus and the C-terminus of the peptide. List all possible peptides that can be formed from the given peptide (use three character/letter abbreviations for each amino acid, i.e., Ala-Gly-Val). NOTE: Any excess will be deducted to the correct answers. Be careful in evaluating your answers.
Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?

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A peptide was cleaved into two smaller peptides with cyanogen bromide (CNBr) and into two different peptides by trypsin (Tryp). Their sequences were as follows: CNB1 1: Gly-Thr-Lys-Ala-Glu CNB 2: Ser-Met Tryp 1: Ser-Met-Gly-Thr-Lys Tryp 2: Ala-Glu What was the sequence of the original peptide?