Deduce the sequence of a heptapeptide that contains the amino acids Ala, Arg, Glu, Gly, Leu,Phe, and Ser, from the following experimental data. Edman degradation cleaves Leu from theheptapeptide, and carboxypeptidase forms Glu and a hexapeptide. Treatment of the heptapeptidewith chymotrypsin forms a hexapeptide and a single amino acid. Treatment of the heptapeptidewith trypsin forms a pentapeptide and a dipeptide. Partial hydrolysis forms Glu, Leu, Phe, and thetripeptides Gly-Ala-Ser and Ala-Ser-Arg.

Amino acid are the organic compounds which contains both amines and carboxylic acids within the…

Answered: Deduce the sequence of a heptapeptide…

Organic And Biological Chemistry

7th Edition

ISBN:9781305081079

Author:STOKER, H. Stephen (howard Stephen)

Publisher:STOKER, H. Stephen (howard Stephen)

Chapter9: Proteins

Section: Chapter Questions

Problem 9.58EP

See similar textbooks

Similar questions

Propose two structures for a tripeptide that gives Leu, Ala, and Phe on hydrolysis but does not react with phenyl isothiocyanate.
Deduce the sequence of a heptapeptide that contains the amino acids Ala, Arg, Glu, Gly, Leu, Phe, and Ser, from the following experimental data. Edman degradation cleaves Leu from the heptapeptide, and carboxypeptidase forms Glu and a hexapeptide. Treatment of the heptapeptide with chymotrypsin forms a hexapeptide and a single amino acid. Treatment of the heptapeptide with trypsin forms a pentapeptide and a dipeptide. Partial hydrolysis forms Glu, Leu, Phe, and the tripeptides Gly–Ala–Ser and Ala–Ser–Arg.
Deduce the sequence of a pentapeptide that contains the amino acids Ala, Glu, Gly, Ser, and Tyr, from the following experimental data. Edman degradation cleaves Gly from the pentapeptide, and carboxypeptidase forms Ala and a tetrapeptide. Treatment of the pentapeptide with chymotrypsin forms a dipeptide and a tripeptide. Partial hydrolysis forms Gly, Ser, and the tripeptide Tyr–Glu–Ala.
Reaction of a polypeptide with carboxypeptidase A releases Met. The polypeptide undergoes partial hydrolysis to give the following peptides. What is the sequence of the polypeptide? 1. Ser, Lys, Trp 4. Leu, Glu, Ser 7. Glu, His 10. Glu, His, Val 2. Gly, His, Ala 5. Met, Ala, Gly 8. Leu, Lys, Trp 11. Trp, Leu, Glu 3. Glu, Val, Ser 6. Ser, Lys, Val 9. Lys, Ser 12. Ala, Met
An octapeptide contains the following amino acids: Arg, Glu, His, Ile, Leu, Phe, Tyr, and Val. Carboxypeptidase treatment of the octapeptide forms Phe and a heptapeptide. Treatment of the octapeptide with chymotrypsin forms two tetrapeptides, A and B. Treatment of A with trypsin yields two dipeptides, C and D. Edman degradation cleaves the following amino acids from each peptide: Glu (octapeptide), Glu (A), Ile (B), Glu (C), and Val (D). Partial hydrolysis of tetrapeptide B forms Ile–Leu in addition to other products. Deduce the structure of the octapeptide and fragments A–D.
Determine the amino acid sequence of a polypeptide from the following data:Acid-catalyzed hydrolysis gives Ala, Arg, His, 2 Lys, Leu, 2 Met, Pro, 2 Ser, Thr, and Val.Carboxypeptidase A releases Val.Edman’s reagent releases PTH-Leu.Trypsin-catalyzed hydrolysis gives three peptides and a single amino acid:1. Arg, Leu, Ser 3. Lys2. Met, Pro, Ser, Thr, Val 4. Ala, His, Lys, Met
Determine the amino acid sequence of a polypeptide from the following data: Complete hydrolysis of the peptide yields Ala, Arg, Gly, 2 Lys, Met, Phe, Pro, 2 Ser, Tyr, and Val. Treatment with Edman’s reagent releases PTH-Val. Carboxypeptidase A releases Ala. Treatment with cyanogen bromide yields the following two peptides: 1. Ala, 2 Lys, Phe, Pro, Ser, Tyr 2. Arg, Gly, Met, Ser, Val Treatment with trypsin yields the following three peptides: 1. Gly, Lys, Met, Tyr 2. Ala, Lys, Phe, Pro, Ser 3. Arg, Ser, Val Treatment with chymotrypsin yields the following three peptides: 1. 2 Lys, Phe, Pro 2. Arg, Gly, Met, Ser, Tyr, Val 3. Ala, Ser
Determine the amino acid sequence of a polypeptide from the following data: Acid-catalyzed hydrolysis gives Ala, Arg, His, 2 Lys, Leu, 2 Met, Pro, 2 Ser, Thr, and Val. Carboxypeptidase A releases Val. Edman’s reagent releases PTH-Leu. Treatment with cyanogen bromide gives three peptides with the following amino acid compositions: 1. His, Lys, Met, Pro, Ser 2. Thr, Val 3. Ala, Arg, Leu, Lys, Met, Ser Trypsin-catalyzed hydrolysis gives three peptides and a single amino acid: 1. Arg, Leu, Ser 2. Met, Pro, Ser, Thr, Val 3. Lys 4. Ala, His, Lys, Met
Determine the amino acid sequence of a polypeptide from the following data:Acid-catalyzed hydrolysis gives Ala, Arg, His, 2 Lys, Leu, 2 Met, Pro, 2 Ser, Thr, and Val.Carboxypeptidase A releases Val.Edman’s reagent releases PTH-Leu.Treatment with cyanogen bromide gives three peptides with the following amino acid compositions:1. His, Lys, Met, Pro, Ser 2. Thr, Val 3. Ala, Arg, Leu, Lys, Met, Ser
Outline the steps needed to synthesize the tetrapeptide Ala–Leu–Ile–Gly using the Merrifield technique.
Researchers analysed a glycopeptide (a peptide carrying one or several oligosaccharide groups) and determined both the sequence of the peptide and the sequence of the sugar molecule. The latter was identified as a diholoside coupled to the peptide by an osidic bond. The systematic name of this sugar is: B-D-glucopyranosyl-(1→4)-ß-D-galactopyranose. : Represent the chemical formula of this diholoside in a way that all oses are Question 1 represented according to the Haworth convention. Apart from the furane and/or pyrane cycles all atoms of this molecule must be given.
A normal polypeptide and a mutant of the polypeptide were hydrolyzed by an endopeptidase under the same conditions. The normal and mutant poly peptide differ by one amino acid. The fingerprints of the peptides obtained from the two polypeptides are shown below. What kind of amino acid substitution occurred as a result of the mutation? (That is, is the substituted amino acid more or less polar than the original amino acid? Is its pI lower or higher?)

SEE MORE QUESTIONS

Recommended textbooks for you

Organic And Biological Chemistry

Chemistry

ISBN:

9781305081079

Author:

STOKER, H. Stephen (howard Stephen)

Publisher:

Cengage Learning,

General, Organic, and Biological Chemistry

Chemistry

ISBN:

9781285853918

Author:

H. Stephen Stoker

Publisher:

Cengage Learning

Organic Chemistry

Chemistry

ISBN:

9781305580350

Author:

William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Publisher:

Cengage Learning

Organic And Biological Chemistry

Chemistry

ISBN:

9781305081079

Author:

STOKER, H. Stephen (howard Stephen)

Publisher:

Cengage Learning,

General, Organic, and Biological Chemistry

Chemistry

ISBN:

9781285853918

Author:

H. Stephen Stoker

Publisher:

Cengage Learning

Organic Chemistry

Chemistry

ISBN:

9781305580350

Author:

William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Publisher:

Cengage Learning

Organic Chemistry

Chemistry

ISBN:

9781305080485

Author:

John E. McMurry

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS