A pentapeptide was found to increase the rate of hydrolysis of fats in the adipose tissues to provide fatty acids as source of energy. The amino acid sequence of this peptide was determined to be: ALA-ARG-LYS-MET-SER Hydrolysis of the three variants of the peptide, and analysis of their amino acid composition revealed the following changes Variants Amino Acid Replacement Peptide 1 Arg was replaced by Leu Peptide 2 Ala was replaced by Tyr Peptide 3 Arg was replaced by Glu What will be the positions of these variant peptides compared with the normal peptide in an electrophoretic run at pH 7.0?

A pentapeptide was found to increase the rate of hydrolysis of fats in the adipose tissues to provide fatty acids as source of energy. The amino acid sequence of this peptide was determined to be: ALA-ARG-LYS-MET-SER Hydrolysis of the three variants of the peptide, and analysis of their amino acid composition revealed the following changes Variants Amino Acid Replacement Peptide 1 Arg was replaced by Leu Peptide 2 Ala was replaced by Tyr Peptide 3 Arg was replaced by Glu What will be the positions of these variant peptides compared with the normal peptide in an electrophoretic run at pH 7.0?

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 18QP: The following is a portion of a protein: met-trp-tyr-arg-gly-pro-thr-Various mutant forms of this...

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The following steps were performed using enzyme cleavage of a peptide to determine its amino acid sequence. Step 1. FDNB yield DNB-Gly Step 2. Treatment with trypsin yield 3 fragments: Tyr-Leu-Asp-Arg; Gly-Ser-Ala-Lys; Trp-Gly-Ser-Met Step 3. Treatment with pepsin gave the same 3 peptide fragments. What is the sequence of the peptide?
A normal polypeptide and a mutant of the polypeptide were hydrolyzed by an endopeptidase under the same conditions. The normal and mutantpolypeptide 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?) (Hint: Photocopy the fingerprints, cut them out, and overlay them.)
Consider the following peptide: Lys-His-Asp-Glu-Phe-Cys-Ala-Asp-His-Arg What is the net charge of this peptide at pH = 1? What is the net charge of this peptide at pH = 14?
The sequence of a 29 aa long peptide can be determined from the following data: Treatment of the peptide with dansyl chloride reveals that the amino-terminal is Val. Trypsin digestion, separation of peptides, and Edmann technique give the sequences for peptide fragments as follows: T-1 V-G-A-H-A-G-E-Y-G-A-E-A-T-E T-2 A-A-W-G-KT-3 V-L-S-P-A-K T-4 T-N-V-K
A heptapeptide when treated with trypsin produced two peptides. T1 (D, G, Y) and T2 (K, F, V, A). When the heptapeptide was treated with chymotrypsin, three peptides were produced: CT1 (K,,Y, G), CT2 (F,A, V), and CT3 (D). The sequences of these peptides is not known, however. When the peptide was treated with Sanger’s Reagent and hydrolyzed, DNP-K and DNP-A were recovered. What is the amino acid sequence of the heptapeptide?
When the amino acid sequences of insulin isolated from differentorganisms were determined, some differences were noted.For example, alanine was substituted for threonine, serine wassubstituted for glycine, and valine was substituted for isoleucineat corresponding positions in the protein. List the single-basechanges that could occur in triplets to produce these amino acidchanges.
The folding of intrinsically disordered proteins is prevented by the presence of Ser, Lys, and Glu residues. What do these amino acids have in common? Why do they disrupt IDPs?
A peptide composed of 40 amino acids (aa) was isolated from the venom of the Gila Monster(Heloderma suspectum, then submitted to various biochemical and chemical treatments.1) After a treatment with a highly specific chymotrypsin, four peptides were generated:- peptide A (6 aa)- peptide B (16 aa)- peptide C (3 aa)- , and peptide D (15 aa)2) Treatment with carboxypeptidases A or B resulted in the release of:- phenylalanine for peptides A and B- tryptophan for peptide C- glycine for peptide D and the 40 amino acids venom peptide3) One cycle of Edman degradation either for peptide A or for the 40 amino acidspeptide gave the exact PTH derivative indicated below: 4) The 40 amino acids peptide treated with Asp-N endopeptidase followed by massspectrometry MS/MS revealed the following composition:- two molecules of glutamic acid,- various peptides indicated below sorted by masses:HG,DLSKQM,EGTFTS,EAVRLFI,EWLKNGGPSSGAPPPSG Information- Chymotrypsin (endopeptidase) hydrolyzes peptide bonds on…
Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide. I don't understand how the order of amino acids in Step 2 was arranged. Please explain. Thank you.
A sample of a peptide of unknown sequencewas treated with trypsin; another sample of the same peptide wastreated with chymotrypsin. The sequences (N-terminal to C-terminal)of the smaller peptides produced by trypsin digestion were as follows:
Digestion of a peptide with trypsin generates two smaller peptide products: methionine-glycine and tyrosine-lysine. Digestion of the same peptide with cyanogen bromide (CNBr) also generates two smaller peptide products: glycine and tyrosine-lysine-methionine. What is the sequence of the original peptide? a.) tyrosine-lysine-methionine-glycine b.) methionine-glycine-tyrosine-lysine c.) glycine-tyrosine-lysine-methionine d.) tyrosine-glycine-methionine-lysine
Treatment of a polypeptide with 2-mercaptoethanol yields two polypeptides 1. Ile—Val—Cys—Arg—Thr—Gly—Cys—Lys—Asn—Phe—Leu2. Trp—Lys—Cys—Phe—Arg—His—Thr—Lys—Cys—SerTreatment of the intact polypeptide with trypsin yields fragments with the following aminoacid compositions(Arg, Cys2, Ile, Ser, Val)(Arg, Cys2, Gly, Lys, Thr, Phe)(Asn, Leu, Phe)(His, Lys, Thr)(Lys, Trp)Edmands chemistry reveal the following PTH derivatives in equal quantity after cycle 1• PTH--Ile and PTH--Trp a) Rewrite the intact polypeptide, by indicating the positions of the disulfide bonds(Indicate your reasoning) b) How many products do you expect after chymotrypsin cleavage of the intactpolypeptide? c) You are performing an isoelectric focusing experiment (IEF) on a gel with a pH range of 2to 14. Indicate on the diagram below at what point along the gel will peptide 1 abovefocus, in the presence (X) and absence (Y) of DTT. (also show your calculations)