A peptide toxin produced by a red spider was sequenced to study itspotential medical use. Sequencing produced the following results:• Peptide composition is phe x4, arg x1, val x1, glu x1• Treatment of the intact peptide with chymotrypsin gave 2 aminoacids, a dipeptide and a tripeptide.• Streptococcal protease treatment cleaved the peptide to a tripeptideand a tetrapeptide of composition arg1phe2val1.• When the peptide toxin was treated with trypsin, a hexapeptide andphe were obtained.Phe-arg-val-glu-phe-phe-phePhe-glu-phe-phe-val-arg-phePhe-phe-glu-phe-val-arg-pheArg-phe-val-phe-glu-phe-pheVal-phe-phe-glu-phe-arg-phe

Peptides are macro molecules made up of Aminoacids joined by peptide bond. Dipeptide is made up of…

Answered: A peptide toxin produced by a red…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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1. Amino acid analysis of the peptide gave the following residues: Asp Leu Lys Met Phe Tyr. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was C-C-CH2. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys. What is the amino acid sequence for this heptapeptide?
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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…
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Which of the peptide sequences below best matches the hydropathy plot shown? 1. ILYYAGSREDHSGYLIL 2. RAFLILFMTYFLILFLI 3. LHGDQNRERDGHSQERD 4. LIFLAIFPAGSTSEDRR 5. EQSDTERNQHGALIYLI
You are trying to determine the PTMs on your protein of interest, so you set up a mass spectrometry experiment. You get the following data. Starting sequence: PRTEINSKICKASSDER After Trypsin digest, you get the following major peptides and weights from MS: TEINSKICK/1167 Da ASSDER/664 Da a. Which of these peptides is modified? b. What is the modification?
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.
33. Gel filtration chromatography shows that the molecular weight of a protein is 240,000 Daltons. However, when the protein was subjected to SDS-PAGE in the absence of ß- mercaptoethanol, two polypeptides (100,000 Daltons, 140,000 Daltons) were identified. Furthermore, when the protein was subjected to SDS-PAGE in the presence of ß- mercaptoethanol, three polypeptides (100,000 Daltons, 90,000 Daltons, and 50,000 Daltons) were identified. Which of the following statements is true of the protein? A. The protein is composed of three polypeptides. B. The three-dimensional structure of the protein is stabilized by both covalent and non- covalent bonds. C. Both A and B. D. Neither A nor B. 34. What is purpose of SDS in SDS-PAGE? E. To selectively bind the target protein F. To maintain buffer pH in the gel G. To cause the separation of proteins to be on the basis of molecular weight only H. To initiate polymerization of acrylamide to form gel
1a) In MALDI-TOF data, when performing peptide mass mapping search, the number of peptides and the sequence coverage decreases, but protien score increase. Explain b) As the same as part a, the peptide masses and the coverage remain the same, but the protien score increase, explain how this can happen.
10. A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the physiological protein has a molecular weight of 240,000 Daltons. Chromatography in the presence of 6 M urea yields a single peak corresponding to a protein of 60,000 Daltons. Chromatography in the presence of 6 M urea and 10 mM mercaptoethanol yields peaks for proteins of 34,000 Daltons and 26,000 Daltons. What can we learn about protein's tertiary and quaternary structure from this data?
1. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Gly-Trp-Phe-Met-Cys- What is observed when the protein sample is subjected to Millon’s test? Violet interface Red precipitate/solution Brown/black precipitate Yelllow product No observable result 2. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Tyr-Trp-Phe-Cys-Gly - What is observed when the protein sample is subjected to lead sulfide test? Violet interface Red precipitate/solution Brown/black precipitate Yelllow product No observable result
A bloactlve hexapeptide was cleaved by trypsln from a larger proteln. The peptlde was sequenced by treatment with varlOus reagents and enzymes. The results are as follows: a) Treatment with cyan0gen bromlde gave a tetrapeptlde of compositlon asp, trp, cys and met. b) Treatment with chymotrypsln gave a tripeptlde of compositlon asp, trp and cys, a dipeptlde wlth the same C-term and an amlno acld. c) Treatment with streptococcal protease gave a dipeptlde and a tetrapeptlde. The composltion of the peptlde Is lys, trp, asp, cys and met 1. What Is the sequence of the hexapeptlde? 2. What is the pl of thls peptlde?

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