what is the sequence of peptide 1?
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what is the sequence of peptide 1?
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- 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.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…you have isolated the following peptide: His-Ser-Arg- Ala-Glu- Leu- Pro- Gly Calculate the approximate charge of the peptide at Ph 1, 3, 5, 8, 11, 14 AND what is the PI of this peptide?
- The oligopeptide isolated from the brain of an animal has the sequence glu-his-tri-ser-tyr-gly-leu-arg-pro-gly. Determine the total charge of the molecule at pH 3.0; 5.5; 11.0. In which pH range there is the isoelectric point of the peptide?You have isolated the following peptide: His-Ser-Arg-Ala-Glu-Leu-Pro-Gly A) Calculate the approximate charge of this peptide at pH 1, pH 3, pH 5, pH8, pH 11, and pH 14. B) What is the PI of this peptide?you have the following peptide Arg-Ile-Pro-Leu-Asp-Lys-Glu The net charge on this peptide at pH 7.0 is ?. The net charge on this peptide at 1M HCl is ?.
- Write the structure of the following peptides: 1. glycyl alanine 2. tyrosyl alanyl glycine 3. phenylalanyl tyrosyl seryl histidine 4. valyl glycyl cystein 5. seryl methionineVII. Analysis of a peptide antibiotic purified from a strain of Bacillus brevii resulted in the following significant information: Complete hydrolysis of the peptide yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val Molecular weight of the peptide was estimated to be aroung 1,200 Da The peptide failed to undergo hydrolysis when treated with carboxypeptidase Partial hydrolysis and then chromatographic separation of products yielded the following di- and tripeptides: Leu-Phe, Phe-Pro, Orn-Leu, Val-Orn, Val-Orn-Leu, Phe-Pro-Val, Pro-Val-Orn Treament with dinitrofluorobenzene (DNFB) followed by complete hydrolysis yielded only free amino acids and the DNFB-derivatized ornithine at its side chain Using this set of information available to you, deduce the amino acid sequence of this peptide antibiotic. Write your final peptide sequence only using 3-letter abbreviations.You have isolated from a rare fungus an octapeptide that prevents baldness and you wish to determine its amino acid sequence. The amino acid composition is K2, D, Y, F, G, S, A. Reaction of the intact peptide with dansyl chloride yields dansyl-A. Cleavage with trypsin yields peptides whose compositions are: (K, A, S) and (G, F, K) plus a dipeptide. Reaction with chymotrypsin releases free D, a tetrapeptide with composition (k, S, F, A) and a tripeptide whose composition following acid hydrolysis is (G, K, Y). The enzymatic digests are each carried out on the whole, undansylated peptide.What is the sequence?
- Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show them in zig-zag style, from amino to carboxy terminus, with correct stereochemistry Draw the predominant form at pH = 2 Draw the predominant form at pH = 5 Draw the predominant form at pH = 7 Draw the predominant form at pH = 12Treatment 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)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