2 Consider the following peptides: (a) Lys-Leu-Met-Phe-Gln (b) lle-Gly-Thr-Asn-Val (c) Arg-Phe-Leu-His-Lys (d) Tyr-Glu-Gln-Asp-Pro (e) Cys-Val-Asp-Asn-Leu Which one of the peptides would have the greatest solubility at pH 1? (a) (b) (c) (d) (e) Consider the following peptides: (a) Lys-Leu-Met-Phe-Gln (b) lle-Gly-Thr-Asn-Val (c) Arg-Phe-Leu-His-Lys (d) Tyr-Glu-Gln-Asp-Pro (e) Cys-Val-Asp-Asn-Leu Which one of the peptides would have the greatest solubility at pH 14? (a) (b) (c) (d) fol

2 Consider the following peptides: (a) Lys-Leu-Met-Phe-Gln (b) lle-Gly-Thr-Asn-Val (c) Arg-Phe-Leu-His-Lys (d) Tyr-Glu-Gln-Asp-Pro (e) Cys-Val-Asp-Asn-Leu Which one of the peptides would have the greatest solubility at pH 1? (a) (b) (c) (d) (e) Consider the following peptides: (a) Lys-Leu-Met-Phe-Gln (b) lle-Gly-Thr-Asn-Val (c) Arg-Phe-Leu-His-Lys (d) Tyr-Glu-Gln-Asp-Pro (e) Cys-Val-Asp-Asn-Leu Which one of the peptides would have the greatest solubility at pH 14? (a) (b) (c) (d) fol

Organic Chemistry

9th Edition

ISBN:9781305080485

Author:John E. McMurry

Publisher:John E. McMurry

Chapter26: Biomolecules: Amino Acids, Peptides, And Proteins

Section26.6: Peptide Sequencing: The Edman Degradation

Problem 15P: Give the amino acid sequence of hexapeptides that produce the following sets of fragments upon...

See similar textbooks

Similar questions

An unknown decapeptide was isolated and characterized. Complete hydrolysis of this peptide gave : F(2), A,G,C,K,N,T, W and V. Treatment with carboxypeptidase releases A. Reaction with Edman’s reagent gave PTH-T and a nonapeptide. The nonapeptide was treated with trypsin and gave 2 peptides: (V-C-G-A) and (N-FF-W-K). Give the sequence of amino acid in the decapeptide.
After treatment with peroxyformic acid, the peptide hormone vasopressin is partiallyhydrolyzed. The following fragments are recovered. Propose a structure for vasopressin.Phe@Gln@Asn Pro@Arg@Gly # NH2 Cys@Tyr@PheAsn@Cys@Pro@Arg Tyr@Phe@Gln@Asn
The Arg-Gly-Asp tripeptide (RGD) is a well-known tumour targeting peptidemotif. Explain how you would synthesise H-Arg-Gly-Asp-OH, starting fromthe constituent amino acids? Explain all steps that are necessary and discuss amechanism for one side chain protection and one C terminus protection.
The peptide Proline-Serine-Alanine-Phenylalanine-Glutamine is present at pH 7. Draw the peptide and include stereochemistry.
Give the amino acid sequence of hexapeptides that produce the following sets of fragments upon partial acid hydrolysis: (a) Arg, Gly, Ile, Leu, Pro, Val gives Pro-Leu-Gly, Arg-Pro, Gly-Ile-Val (a) N, L, M, W, V2 gives V-L, V-M-W, W-N-V
Calculate an approximate pI for Peptide E-G-E-A
What is the net charge of the following peptide at pH 7.0: E-H-A-S-W-R-C a. +2 b. +1 c. 0 d. -1 e. -2.
Given the following peptideSEPIMAPVEYPK(a) Estimate the net charge at pH 7 and at pH 12. Assume the pKa valuesgiven in Table (b) How many peptides would result if this peptide were treated with(1) cyanogen bromide, (2) trypsin, or (3) chymotrypsin?(c) Suggest a method for separating the peptides produced by chymotrypsintreatment.
Somatostatin is a tetradecapeptide of the hypothalamus that inhibits the release of pituitary growth hormone. Its amino acid sequence has been determined by a combination of Edman degradations and enzymic hydrolysis experiments. On the basis of the following data, deduce the primary structure of somatostatin: 1. Edman degradation gave PTH-Ala. 2. Selective hydrolysis gave peptides having the following indicated sequences: Phe-Trp Thr-Ser-Cys Lys-Thr-Phe Thr-Phe-Thr-Ser-Cys Asn-Phe-Phe-Trp-Lys Ala-Gly-Cys-Lys-Asn-Phe 3. Somatostatin has a disulfide bridge.
A nonapeptide released by globulins in the blood in response to a waspsting. Hydrolysis gives the following amino acids: 2 Arg, Gly, 2 Phe, 3 Pro, and Ser.Edman degradation gives phenylthiohydantoin of Arg. Cleavage with carboxypeptidase gives Arg. Partial hydrolysis gives the following di- and tripeptides: Phe-Ser, Pro-GlyPhe, Pro-Pro, Ser-Pro-Phe, Phe-Arg, and Arg-Pro. What is the amino acid sequence of this peptide?
Consider the peptide EAHIVR. Write out the sequence of the peptide from N to C in three letter code. Draw the complete structure of the peptide including all peptide bonds and side chains at pH 8.0. Calculate the pI of this peptide. Calculate the net charge of this peptide at pH 2, pH 7, and pH 11. *please show math for # 3 and #4 pls*
Explain why the pKa of the - NH3+ group of an a-amino acid is lower than the pKa of the ammonium ion derived from a 1° amine (RNH3+). For example the pKa of the - NH3+ group of alanine is 9.87 but the pKa of CH3NH3+ is 10.63.