A NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare fungus. Amino acid analysis of the peptide reveals the followinginformation below: (NOTE: when the sequence is not known, a comma separates the amino acids)HydrezineNonapeptideAcid Hydrolysis (4 N HCI) at 110 C(2) Arg. Gin, (2) Tyr, Gly, Ser, Thr, and Met2,4-dinitrolluorobenzeneDNP-ThrGin andPeptide 1(Arg. Thr, Ser)modified freeamino acidsCleavoge with Trypsin, then thrometographyPeptide 2(Gly, Tyr, Arg)MetTripeptide(yenegen bromideDipeptideCleovoge with Chymetrypsin, then chromatographyPeptide 3(Arg, Ser, Tyr, Thr)Amino acidPeptide 4(Gly, Arg, Tyr)When answering the questions below, please use the one-letter code for the amino acid, with NO spaces and symbols between each letter.1. What is the N-terminal AA residue?2. What is the C-terminal AA residue?3. What is the sequence of Peptide 1?4. What is the sequence of Peptide 4?5. What is the overall amino acid sequence?

DNA sequencing is a biochemical method for determining the order of the nucleotide bases, adenine,…

Answered: A NONAPEPTIDE that attacks and kills…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 14QP: If phenylalanine was not an essential amino acid, would diet therapy (the elimination of...

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A NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare fungus. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrazine Acid Hydrolysis (6 N HCI) at 110 "C Nonapeptide (2) Arg, Gln, (2) Tyr, Gly, Ser, Thr, and Met 2,4-dinitrofluorobenzene DNP-Thr Gin and modified free Peptide 1 (Arg, Thr, Ser) amino acids Cleavage with Trypsin, then chromatography Peptide 2 (Gly, Tyr, Arg) Met Tripeptide Cyanogen bromide Dipeptide Peptide 3 (Arg, Ser, Tyr, Thr) Cleavage with Chymotrypsin, then chromatography Amino acid Peptide 4 (Gly, Arg, Tyr)
Draw the structure of the PTH derivative product you would obtain by Edman degradation of the following peptides: (a) I-L-P-F (b) D-T-S-G-A
(a) A decapeptide has the following amino acid composition: Alaz, Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides: Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly. Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine om the experimental data, deduce the primary structure of the decapeptide.
H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14
A decapeptide was isolated from a thermophilic bacteria. Treatment of this peptide with 2- mercaptoethanol gave 2 pentapeptides. Further analysis of this peptide gave the following data: Trypsin: (M,Y), (K,Y,M), (K, 2A, 2C) Chymotrypsin: (2K, 2A, 2C, Y), (M), (Y,M) What is the primary structure of the decapeptide? Thank you.
Given the following peptides below, what would be more soluble at the indicated pH? 1. (Gly)20 or (Glu)20 in pH 7.0 2. (Lys-Ala)3 or (Phe-Met)3 in pH 7.0 3. (Gly)20 or (Glu)20 in pH 6.0|| 4. (Ala-Ser-Gly)s or (Asn-Ser-His)s in pH 6.0 5. (Ala-Asp-Gly)8 or (Asn-Ser-His)8 in pH 3.0
What is the charge on the following peptide at standard biochemical pH? S-Y-D-F-K-I-V-F-L-L +2 -1 0 0 0-2 O +1
For the following pentapeptides: Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser Draw the most protonated forms of the pentapeptides Illustrate the ionization of the pentapeptides from the most protonated to its deprotonated form. Label the ionization with its respective pK values. Compute their isoelectric pH (pI). Do these peptides with the same amino acid composition have different net charges at pH 7.0? Explain briefly. Would you expect the titration curves of the two peptides to differ? Why or Why not?
A nonapeptide was determined to have the following amino acid composition: (Lys)2, (Gly) 2, (Phe) 2, His, Leu, Met. The native peptide was incubated with 1-fluoro-2,4- dinitrobenzene (FDNB) and then hydrolyzed; 2,4-dinitrophenylhistidine was identified by HPLC. When the native peptide was exposed to cyanogen bromide (CNBr), an octapeptide and free glycine were recovered. Incubation of the native peptide with trypsin gave a pentapeptide, a tripeptide, and free Lys. 2,4-Dinitrophenyl-histidine was recovered from the pentapeptide, and 2,4-dinitrophenylphenylalanine was recovered from the tripeptide. Digestion with the enzyme pepsin produced a dipeptide, a tripeptide, and a tetrapeptide. The tetrapeptide was composed of (Lys) 2, Phe, and Gly. The native sequence was determined to be: Met-Leu-Phe-Lys-Phe-Gly-Gly-Lys-His His-Leu-Gly-Lys-Lys-Phe-Phe-Gly-Met His-Phe-Leu-Gly-Lys-Lys-Phe-Met-Gly Gly-Phe-Lys-Lys-Gly-Leu-Met-Phe-His ● His-Leu-Phe-Gly-Lys-Lys-Phe-Met-Gly
Hydrolysis of dodecapeptide P with the enzyme trypsin affords the following fragments: Arg, Ser-Tyr-Ser-Met-Lys, Ala-Gly-Asp-Phe-Glu-Arg. Hydrolysis with chymotrypsin yields: Glu-Arg, Arg-Ser-Tyr, Ser-Met-Lys-Ala-Gly-Asp- Phe. What is the amino acid sequence of P? Submit Answer Retry Entire Group 9 more group attempts remaining
For the dipeptide Arg–His, find the pI (the pKs are α-amino 9.0, guanidino 12.5, imidazole 6.0, α-carboxylate 2.1).
The oligopeptide isolated from the brain of an animal has the sequence glu-his-tri-ser-tyr-gly-leu-arg-pro-gly. Determine the total charge of the molecule at pH 3.0; 5.5; 11.0. In which pH range there is the isoelectric point of the peptide?

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