Which of the following peptides are consistent with the data below? 1. Amino acid analysis gave Met, His, Glu, Lys, Tyr, Val 2. Treatment of the peptide with trypsin led to a tetrapeptide and a dipeptide. 3. Treatment with cyanogen bromide gave a tetrapeptide and a dipeptide. 4. Edman degradation gave the following compound (shown). HN- HO- S= 'N' O Tyr-Lys-His-Glu-Val-Met O Tyr-Met-His-Lys-Glu-Val O Tyr-Lys-His-Glu-Met-Val O Val-Met-Glu-Lys-His-Tyr 5.
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- 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?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…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
- A peptide was analyzed with the following results. Whatis the primary sequence of the peptide? Briefly state the conclusions of each experimental result and indicate your logic. a)Mass spectrometry was consistent with a peptide of 7 amino acids containing W,C,D,M,N,K, and I. b)One cycle of Edman degradation of the peptide yielded a single product, the PTH derivative of I c)Cleavage of the peptide with CNBr yielded two products. One contained 5 amino acids, and the other 2. One cycle of Edman degradation yielded the PTH derivatives of Iand N, respectively. d)Treatment of the peptide with trypsin yielded 2 products. One of them had significant light absorbance at 280 nm, and Edman degradation yielded the PTH derivative of I. The other trypsin-generated product contained 4 amino acids, and Edman degradation yielded the PTH derivative of Asp.Determine the Primary amino acid sequence of an Octapeptide Composition · Tyr , Arg,Pro, Lys ,Lys ,Met ,Trp,Phe N terminal 1 2 3 4 5 6 7 8 C terminal 1) Treatment with an Edman reagent gives a PTH-AA that shows a Yellow color with Ninhydrin. 2) Trypsin digestion of the Octapeptide gives tetepeptide, dipeptide, free Arg ,free Trp. 3)CNBr = pentapeptide and tripeptide. 4) chymotrysin - tetapeptide and two dipeptiele. The tetrapeptide contains an amino acid with an OH group in the side chain.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)
- Examine the following peptide and the inserted table, and answer the 2 questions below: Thr-Glu-Pro-Ile-Val-Ala-Pro-Met-Glu-Tyr-Gly-Lys 1. Estimate the net charge of the peptide at pH 2.0. Explain. 2. Estimate the net charge of the peptide at pH 7.0. Explain.The following data describe the catalysis of cleavage of peptide bonds in small peptides by the enzyme UTSAse (the arrow indicates the peptide bond cleaved in each case). Substrate Km(mM) kcat(s-1) PAPA↓G 4.0 26 PAPA↓A 1.5 37 PAPA↓F 0.64 18 what features of amino acid sequence dictate the specificity of the proteolytic cleavage? Large hydrophilic R-groups Large hydrophobic R-groups Neutral R-groups Small hydrophilic R-groups Large hydrophobic R-groups Negatively charged R-groups Positively charged R-groupsZ-scale descriptors are also calculated for artificial (synthetic) amino acids. Which of the four following descriptions could correspond to amino-phenylacetate and which to homoarginine? Justify your answer! 1) z1=-3.51 z2=2.93 z3=2.94 2) z1=2.70 z2=3.06 z3=-4.15 3) z1=-3.51 z2=-2.93 z3=2.94 4) z1=2.70 z2=-3.06 z3=
- VII. 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.In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These messages yielded proteinswith the amino acid compositions shown in the followingtable. Using these data, predict the most specific coding compositionfor each amino acid.4/5C:1/5A 4/5A:1/5CPro 63.0% Pro 3.5%His 13.0% His 3.0%Thr 16.0% Thr 16.6%Glu 3.0% Glu 13.0%Asp 3.0% Asp 13.0%Lys 0.5% Lys 50.0% 98.5% 99.1%Determine the amino acid sequence of a polypeptide from the following data:Complete hydrolysis of the peptide yields Arg, 2 Gly, Ile, 3 Leu, 2 Lys, 2 Met, 2 Phe, Pro, Ser, 2 Tyr, and Val.Treatment with Edman’s reagent releases PTH-Gly.Carboxypeptidase A releases Phe. Treatment with trypsin yields the following four peptides:1. Gly-Leu-Tyr-Phe-Lys 3. Val-Ile-Arg2. Ser-Met-Gly-Leu-Tyr-Lys 4. Met-Leu-Pro-Phe