13. Amino acid analysis of a seven residue long peptide gaveAspLeuArgMet | PheMet | Phe | Tyr(i) The PTH amino acid derivative released by Edman degradation was Tyr-PTH(ii) Trypsin treatment had no effect(iii) Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free Arg(iv) Brief chymotrypsin treatment yielded several products, including a dipeptide and a tetrapeptide.The amino acid composition of the tetrapeptide was Leu, Arg, and MetWhat is the amino acid sequence of this seven residue long peptide, and explain how youreached that conclusion?

ANSWER:Tyr - Asp - Phe - Met - Leu - Arg - X The amino acid sequence of the seven-residue long…

Answered: 13. Amino acid analysis of a seven…

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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A At pH 5, what is the net charge of the peptide Val-His-Gln-Cys-Ser-Lys? 0 -1 0 0+1 Ⓒ +2 Q Search "de 96 5 ******* ******* 131183 J- C 8 a hp
3 of 3 A protein was completely digested with trypsin and an internal peptide (i.e. not derived from the N- or C-terminals) was purified. Determine its sequence from the following information: a) amino acid analysis yields one mole of D, T, P, L, Y, F, K, and R per mole of peptide; b) treatment of the intact peptide with FDNB, followed by acid hydrolysis, gives DNP-L and &-DNP-K; c) treatment of the intact peptide with chymotrypsin yields a tripeptide containing K, T, and D; a tetrapeptide containing P, L, F, and R, and free tyrosine; d) the tripeptide, in part c, yields DNP-T and ɛ-DNP-K after reaction with FDNB and acid hydrolysis. Note: trypsin will not cleave on the carboxyl side of arginine or lysine if the next amino acid (donating the amino group) is proline. Put your answer here:
What is the first thing that must occur in order for the catalysis of the peptide bond to begin. What is a specificity pocket? What are the preferences of chymotrypsin due to its specificity pocket?
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.
5 For the peptide structure in #3, (ASP-ALA-THR-LYS-GLY), use the chart at the end of this HW set to: A. Determine the net charge of the pentapeptide at pH 3, 4, 7, 10 and 11. B. Estimate the isoelectric point, pl, for this 5-amino acid peptide
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?
Which of the peptide sequences below best matches the hydropathy plot shown? 1. ILYYAGSREDHSGYLIL 2. RAFLILFMTYFLILFLI 3. LHGDQNRERDGHSQERD 4. LIFLAIFPAGSTSEDRR 5. EQSDTERNQHGALIYLI
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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.
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
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