Draw the structure of DVPAR in its predominant form as it would exist at pH 5. D (Aspartic acid), V (Valine), P (Proline), A (Alanine), R (Arginine).

Answered: Image /qna-images/answer/72686ca5-4717-40fc-8ea1-1074afd82fe0.jpg

Answered: Draw the structure of DVPAR in its…

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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There is parts A-D for the picture provided. A) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 1? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 B) A peptide has the sequence Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 5? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 C) Same Peptide sequence, What is the net charge at pH8.5, (N-terminus is pronated) Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 D) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 13? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 Thank You!
For each of the following amino acids: 1) describe what the important functional group of the amino acid side chain is, 2) identify the charge of the side chain, 3) name another component in the structure that the amino acid might interact with, and 4) indicate how the interaction with the component listed in 3) might be occurring (i.e., electrostatic interaction, hydrogen bond, hydrophobic interaction, etc.) a) Asp153 b) Arg166 c) Lys167
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?
A HEPTAPEPTIDE that punctures the bacterial cell wall has just been recently isolated from the venom gland of a frog. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrezine Acid Hydrolysis (6 N HC) at 10 C Heptapeptide (2) Arg. Pro, Phe, Tyr, Ala, Lys 2,4 dinitrafluerobenzene DNP-Phe Lys and modified free amino acids Peptide 1 (Ala, Lys) Cleovage with Trypsin, then chrometogrophy Peptide 2 (Pro, Arg, Tyr) Peptide 3 (Phe, Arg) Phe Peptide 4 (Arg. Tyr) Clevege with Chymetrypsin, then cromategrphy Peptide 5 (Lys, Pro, Ala, Arg)
What is the pl of the polypeptide ACYK? Consider the following pKa values: terminal amino group: 9.5; C = 8.2; Y = 10.1; K= 10.5; terminal carboxyl group = 2.5. 5.4 8.9 9.8 O 10.3
what is the N and C terminal AA residue?
A mixture of Asparagine (pl 5.41), Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2: v First 1. Asparagine v Second 2. Aspartic Acid 3. Histidine v Third 4. Lysine v Fourth 5. Threonine v Fifth 6. No separation
Please draw the titration curve Arginine (y-axis: pH, x-axis: moles of OH-). Label the graph with the pKas and pI of the amino acid. Also, draw the species of the Arginine along the titration.
Polypeptide Handout Amino acids are linked together to form a peptide bond through an aminidation reaction. The-COO group of one amino acid reacts with the -NH3+ of another amino acid. When two are more amino acids are linked together a peptide is formed. Draw the Following Polypeptides: a) Gly-Ser-Met-Lys b) Lys-Pro-Val-His c) Trp-Thr-Leu-lle d) Cys-Met-Phe-Glu e) G-L-A-R-E f) G-L-A-D g) F-H-E-D h) K-E-M-S
Please calculate and plot the charge on a peptide with the sequence of NEYK over the pH range from 1 to 13. Please use the pKa values from the table. You may calculate the charge at 1 pH unit intervals.
2) For the following amino acids, encircle those with a net charge of -2 at high pH underline those with +2 at low pH Aspartic acid, Alanine, Arginine, Glutamic acid, Valine, Leucine, Lysine, Isoleucine
Identify the following amino acid at pH = 7 (aqueous form): (COO-)–CH(NH3+)–CH2–(COO-) aspartic acid asparagine histidine arginine lysine

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