When answering the questions below, please use the ONE-LETTER CODE for the aminoacid, with NO spaces and symbols between each letter.1. What is the C-terminal residue?2. What is the N-terminal residue?3. What is the sequence of Peptide 2?4. What is the sequence of Peptide 4?5. What is the overall amino acid sequence? A HEPTAPEPTIDE that punctures the bacterial cell wall has just been recentlyisolated from the venom gland of a frog. Amino acid analysis of the peptide revealsthe following information below: (NOTE: when the sequence is not known, a commaseparates the amino acids)HydrezineAcid Hydrolysis (6 N HC) at 10 CHeptapeptide(2) Arg. Pro, Phe, Tyr, Ala, Lys2,4 dinitrafluerobenzeneDNP-PheLys andmodified freeamino acidsPeptide 1(Ala, Lys)Cleovage with Trypsin, then chrometogrophyPeptide 2(Pro, Arg, Tyr)Peptide 3(Phe, Arg)PhePeptide 4(Arg. Tyr)Clevege with Chymetrypsin, then cromategrphyPeptide 5(Lys, Pro, Ala, Arg)

Trypsin and chymotrypsin are the proteases that break down protein into individual amino…

Answered: When answering the questions below,…

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

Calculate the net charge of the following peptide at pH 2, pH 6 and pH 14 (use 2 and 9 as pKa values for the carboxylic acid and amino groups, respectively, use the attached table for the side chain pKa values). Ile-Leu-Ile-Lys-Glu-Cys-His-Glu-Met-Ile-Ser-Thr-Arg-Tyr
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)
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) 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.
The peptide with sequence GVPLT has antioxidant properties. Draw the chemical structure of this peptide at pH 7
Calculate the pI for the following peptide: Phe-Lys-Glu-Asp-Lys-Ser-Ala (note: there is only one alpha carboxyl at the C terminus and one alpha amino group at the N terminus and don't forget to take into account the ionizable side chain groups)
An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.
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
A mixture of Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74), Phenylalanine (pl 5.48) 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. Aspartic Acid v Second 2. Histidine v Third 3. Lysine 4. Phenylalanine v Fourth 5. Threonine v Fifth 6. No separation
The structure of a peptide is shown below: OH HN NH, How many hydrolytic products will be obtained by cleavage with trypsin, a protease? А. 2 В. 3 О С.4 O D. 5 E. none; trypsin will not cleave the peptide
Phosphoproteins are formed when a phosphate group is esterified to an -OH group of a Ser, Thr, or Tyr side chain. At typical cellular pH values, this phosphate group bears two negative charges (-OPO32-). Compare this side-chain modification to the 20 side chains of the common amino acids found in proteins and comment on the novel properties that it introduces into side-chain possibilities.
Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. List down the different fragments that would result if dynorphin were cleaved by trypsin. . How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. . Cyanogen bromide is a chemical reagent which also cleaves peptide bonds. What is/are…

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