Consider the peptide HRDMQSGAI.Part: 0/5Part 1 of 5Identify the side chains of the amino acid residues in the peptide that are nonpolar. Check all that apply.HRD☐M1QSGNone of the abovex

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Answered: Consider the peptide HRDMQSGAI. Part:…

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 peptide sequences below best matches the hydropathy plot shown? L 10 Residue Number 4 2 Hydropathy value -2 0 セー RAFLILFMTYFLILFLI ILYYAGSREDHSGYLIL OLHGDQNRERDGHSQERD EQSDTERNQHGALIYLI 01 5 15
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At what pH can you separate the following peptides: ala-ala-ala, glu-glu-glu, his-his-his? OA 2.0 B. 4.0 C. 5.0 O D. 7.0 E. 9.5
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I need help with drawing Hydrogen bonding between two tripeptide: Ser-Lys - Ser. In my class, we are required to give dash or wedge for the side chain R in the amino acid, and draw zig zag for the chain. In two separate drawings, can you draw one where it is the hydrogen bonding between the peptides backbone that connect the two tripeptides and the other is the hydrogen bonding between the side chains. Thanks
Consider each dipeptide. Part: 0 / 4 Part 1 of 4 HO || H H H3N C-C-N-C-COO Identify the amino acid(s) present in this structure. Check all that apply. U U U glycine cysteine valine alanine Ophenylalanine ☐ U U asparagine tyrosine threonine leucine glutamine serine ☐ isoleucine methionine None of the above X
Based on the pK, table for amino acids (Table 1.1), draw the structures with net charge, and the equilibria representing the complete deprotonation of aspartate. Table 1.1 Name pK pk2 pKR Glycine Alanine 2.4 9.8 2.3 9.7 Valine 2.3 2.4 9.6 Leucine 9.6 Isoleucine 2.4 9.7 Methionine 2.3 9.2 Phenylalanine Proline Serine 1.8 9.1 2.0 10.6 2.1 9.2 Threonine 2.6 10.4 Cysteine Asparagine Glutamine 1.8 10.8 8.3 2.0 8.8 2.2 9.1 Tyrosine Tryptophan Aspartate Glutamate 2.2 9.1 10.9 2.4 9.4 2.0 2.2 10.0 3.9 9.7 4.3 Histidine 1.8 9.2 6.0 10.8 Lysine Arginine 2.2 9.2 1.8 9.0 12.5
Shown is the electrophoretic profile of a pure protein ran at different pH values HH (+) (-) pH 5 pH 6.5 pH 7.4 pH 9.2 What is most likely the reason for the change in the position of the protein band at pH 9.2? A. deprotonation of internally located basic amino acid residues B. deprotonation of N-terminal amino acid C. deprotonation of an internally located basic amino acid, his D. deprotonation of acidic amino acids, glu and asp E. deprotonation of cys
Draw the structure of the tri-peptide Leu-Asn-Ser at pH 7.4. Use wedges and dashes around the alpha-carbons, and indicate charges where appropriate. Indicate which amino acid(s) has an R group that would avoid water.
+H₂N-CH-COO™ T CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. O amino acid C amino acid D O amino acid E amino acid B +H₂N-CH-COO™ I CH₂ I CH₂ 1 O amino acid A C=0 B. If the pH decreases enough, this amino acid will become protonated and could contribute to the denaturation of the protein. +H₂N-CH-COO™ 1 CH₂ I OH C. +H₂N-CH-COO™ CH H₂C CH3 D.

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Consider the peptide HRDMQSGAI. Part: 0/5 Part 1 of 5 Identify the side chains of the amino acid residues in the peptide that are nonpolar. Check all that apply. H R D ☐ M 1Q S G None of the above x