HCH₂H₂CHC-CH3CH₂HH₂C(S)H₂CHCH₂CH₂CH₂NHOC NHNH₂a) Which of the following statements aboutthis peptide are correct?Group of answer choicesTreatment of this peptide with trypsingenerates two products.This peptide is a substrate forcarboxypeptidase ATreatment of this peptide with cyanogenbromide generates a pentapeptide and atripeptide.Treatment of this peptide with chymotrypsingenerates three products.Treatment of this peptide with elastasegenerates 2 products.None of the above statements are correct.b) What is the sequence of this peptide usingone letter abbreviations?c) What is the pH which would correspond tothe ionization of the peptide as drawn above?1, 5, 7, 10, 14

Recall that:amino acid sequences are written with N-terminal amino acid on the left and C-terminal…

Answered: H CH₂ HỎ=CH. CH₂ H₂C (5) H CH₂ H₂C CH₂…

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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peptide Lys-Glu-Trp answer the following questions: Draw the structure of this peptide when all the ionizable groups are fully protonated. How many ionizable groups does this peptide have? Label the pKa for each of the ionizable groups in the structure above. Draw the appropriate titration curve for this peptide on graph paper starting at pH 0 and ending at pH 14. Label the x-axis, y-axis and the pKa Determine the overall net charge of this peptide at each full equivalent point (including 0) where the ionizable group is 100% deprotonated. Determine the pI for this peptide. Determine the average overall net charge of a mixture of this peptide in a solution where pH=8.5.
The peptide CMYLES is reacted with phenylisothiocyanate under basic conditions followed by incubation with anhydrous trifluoroacetic acid. What are the products of this reaction? PTH-CMYLES Thiazolinone derivative of cysteine, MYLES O PTH-C, PTH-M, PTH-Y, PTH-L, PTH-E, PTH-S PTH-C, MYLES PTH-S, CMYLE
A tetrapeptide, glutamate-glycine-alanine-lysine, is prepared at at concentration of 1 mM (0.001 M) and is measured in the standard setup (pathlength of 1 cm). What is the approximate absorbance of this peptide at 280 nm? Hint: if the peptide contained a single tryptophan, the answer would be about 10. 10 280 1 0
the following peptide is incubated as chymotrypsin: Gly-Val-Phe-Lys-Ala. Present the detailed chemical mechanism by which chymotrypsin hydrolyzes this peptide. Briefly explain each step. Include only the structure of the final products of the reaction.
Draw the structure of the PTH derivative you would obtain by Edman degredation of the peptide: ALPF.
On the basis of the information provided in Figure 9.17, complete the mechanisms for peptide-bond cleavage by (a) a cysteine protease, (b) an aspartyl protease, and (c) a metalloprotease.
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 8. 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. 9. List down the different fragments that would result if dynorphin were cleaved by trypsin. 10. 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. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. 12. Cyanogen bromide is a chemical reagent which also cleaves peptide bonds.…
A mutant form of polypeptide hormone angiotensin II has the amino acid composition (Asp, Arg, Ile, Met, Phe, Pro, Tyr, Val) The following observations are made: Trypsin yields a dipeptide containing Asp and Arg, and a hexapeptide with all the rest. • Cyanogen bromide cleavage yields a dipeptide containing Phe and Pro, and a hexapeptide containing all the others. • Chymotrypsin cleaves the hormone into two tetrapeptides, of composition (Asp, Arg, Tyr, Val) and (Ile, Met, Phe, Pro) • The dipeptide of composition (Pro, Phe) cannot be cleaved by either chymotrypsin or carboxypeptidase. What is the sequence of angiotensin II?
Name three biologically active peptides. Mention their functions.
A decapeptide was analyzed and the following information obtained. Determine the primary structure of the peptide. Edman's Degradation: PTH-Ala Trypsin produces 3 peptides of the following composition: 1. Gly, His 2. Ala, Leu, Lys, Val 3. Arg (2), Phe, Pro Chymotrypsin produces 2 peptides of the following composition: 1. Ala, Leu, Lys, Phe, Val 2. Arg (2), Gly, His, Pro Elastase produces 1 amino acids and 3 peptides 1. Ala 2. Leu, Val 3. Arg (2), Lys, Phe, Pro, Gly, His Arg Gly His Leu Phe Pro Val
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
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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