3) The following is the amino acid sequence of bradykinin, a peptidereleased by certain organisms in response to wasp stings:Arg – Pro – Pro - Gly – Phe – Ser – Pro – Phe – ArgWhat amino acids or peptides are produced when bradykinin istreated with each of the following reagents?a) with Carboxypeptidase c) with Trypsinb) with Chymotrypsin d) with DNFB

Answered: 3) The following is the amino acid…

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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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.
Predict the fragments that will be generated from the treatment of the following peptide with: a) trypsin; b) chymotrypsin; c) and S. aureus V8 protease: Gly-Ala-Trp-Arg-Asp-Ala-Lys-Glu-Phe-Gly-Gln
Hydrolysis of β-endorphin (a peptide containing 31 amino acid residues) produces the following amino acids: Tyr 1), Gly 3), Phe 2), Met, Thr 3), Ser 2), Lys 5), Gin 2), Pro, Leu 2), Val 2), Asn 2), Ala 2), lle, His, and Glu Treatment with carboxypeptidase liberates Gln. Treatment with DNFB liberates DNP-Tyr. Treatment with trypsin produces the following peptides: Lys, Gly—Gln, Asn—Ala—He—Val—Lys, Tyr—Gly—Gly—Phe—Met—Thr—Ser—Glu—Lys, Asn—Ala—His—Lys, Ser—Gln—Thr—Pro—Leu— Val—Thr—Leu—Phe—Lys Treatment with chymotrypsin produces the following peptides: Lys—Asn—Ala—He—Val—Lys—Asn—Ala—His—Lys—Lys—Gly—Gln Tyr—Gly—Gly—Phe Met—Thr—Ser—Glu—Lys—Ser—Gin—Thr—Pro—Leu—Val—Thr—Leu—Phe What is the primary sequence of β-endorphin?
You have isolated this peptide. AÇQGRKSPWTT TAHEVYPGGČMN What products would you get if you treated with: a) DTT ( dithiothreitol) b) Trypsin c) Carboxypeptidase A ( 1 cycle) d) Aminopeptidase M ( 2 cycles) e) DTT, then Iodoacetate, then elastase
1. Amino acid analysis of the peptide gave the following residues: Asp Met The following facts were observed: a) Trypsin treatment had no effect. b) The phenylthiohydantoin released by Edman degradation was Leu Lys Phe Tyr What is the amino acid sequence for this heptapeptide? H C-C-CH₂ H c) Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. d) Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys.
Deduce the amino acid sequence of a polypeptide from the following:1. Acid hydrolysis gives Ala2, Arg, Lys2, Met, Phe, Ser22. Carboxypeptidase gives Ala3. Trypsin digestion gives 4 peptides a) Ala, Arg b) Lys, Phe, Ser c) Lys d) Ala, Met, Ser4. CNBr treatment gives a) Ala, Arg, Lys2, homoserine, Phe, Ser b) Ala, Ser5. Thermolysin is a protease that cuts on the N-terminal side of hydrophobic amino acids (substrate preference is Leu, Ile, Phe, Trp, Tyr, Val). Thermolysin treatment of our polypeptide yields 2 peptides a) Ala, Arg, Ser b) Ala, Lys2, Met, Phe, Ser
1. Label the ALPHA-Carbon, AMINO Group, CARBOXYL Group, and AMINO Side Chain of the following amino acids:- Proline- Glycine- Aspartic acid- Asparagine- Lysine 2. Write the structure of the following polypeptide chainsa.) Asp-Leu-Serb.) Thr-Trpc.) Gln-Ala-Prod.) Ile-Met-Cys-Glu
Given the peptide Lys-Glu-Trp a) Draw the appropriate titration curve for this peptide. Label X and Y axis b) On the graph use X to mark point at which peptide have 0 net charge and Y to mark point where peptide have positive 1 net charge
Amino acid analysis of the peptide angiotensin II shows the presence of eight different aminoacids in equimolar amounts: Arg, Asp, His, Ile, Phe, Pro, Tyr and Val. Partial hydrolysis ofangiostensin II with dilute HCl yields the following fragmentsa.) Asp –Arg- Val –Tyr b.) Ile –his –Proc.) Pro –Phe d.) Val – tyr – Ile –His a.)What is the sequence of angiostensin II and what Fragment would result if angiotensin II were cleaved with trypsin? Withchymotrypsin?
Consider the following peptide: Lys-Tyr-Glu-His-Arg-Ala-Asp-Arg-Glu-Tyr-Lys a) What is the net charge of this peptide at pH=1? Show your work. b) What is the net charge of this peptide at pH=14? Show your work.
What products are formed when each peptide is treated with trypsin? Be sure to answer all parts. [1] Phe-Leu-Phe-Asn-Lys-Ser [2] Phe-Ser-Thr-Arg-His-Trp [3] Met-Met-Lys-Val-Asp-His-Thr-Thr-Tyr-Ala-Thr-Glu

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