A nonapeptide was determined to have the following amino acid composition: (Lys)2, (Gly) 2,(Phe) 2, His, Leu, Met. The native peptide was incubated with 1-fluoro-2,4- dinitrobenzene(FDNB) and then hydrolyzed; 2,4-dinitrophenylhistidine was identified by HPLC. When thenative peptide was exposed to cyanogen bromide (CNBr), an octapeptide and free glycinewere recovered. Incubation of the native peptide with trypsin gave a pentapeptide, atripeptide, and free Lys. 2,4-Dinitrophenyl-histidine was recovered from the pentapeptide,and 2,4-dinitrophenylphenylalanine was recovered from the tripeptide. Digestion with theenzyme pepsin produced a dipeptide, a tripeptide, and a tetrapeptide. The tetrapeptide wascomposed of (Lys) 2, Phe, and Gly. The native sequence was determined to be:Met-Leu-Phe-Lys-Phe-Gly-Gly-Lys-HisHis-Leu-Gly-Lys-Lys-Phe-Phe-Gly-MetHis-Phe-Leu-Gly-Lys-Lys-Phe-Met-GlyGly-Phe-Lys-Lys-Gly-Leu-Met-Phe-His● His-Leu-Phe-Gly-Lys-Lys-Phe-Met-Gly

Trypsin - Cleaves at Carboxyl terminus of basic amino acid such as lysine and arginine. Ahead of…

Answered: A nonapeptide was determined to have…

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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An octapeptide was hydrolyzed and the amino acids separated. Its amino acid composition was determined: Gly (1); Ala (2); Val (1); Lys (2); Met (1); Asp (1). After incubation with FDNB and hydrolysis, 2,4-dinitrophenylalanine was detected. NO2 H H N C COOH ON- CH, Treatment with cyanogen bromide, which cleaves at M, resulted in two fragments: a pentapeptide containing two K residues and a tripeptide containing V, G, and A. The residues are not listed in any particular order. After treatment with trypsin, which cleaves at R and K, there were three fragments: two dipeptides and MGAV. What is the sequence of the octapeptide? Use the one-letter abbreviations for the amino acids, and do not use dashes.
A peptide with endorphin-like property was produced and obtained from the blood. This was sequence using the protocol: Treatment with streptococcal protease gave a tripeptide and a tetrapeptide. Treatment with trypsin gave two tripeptides and an amino acid. Treatment of the 2 tripeptide products in 1.2 with 2,4-dinitrophenol gave DNP- S, and DNP-E and a mixture of amino acids. The composition of the peptide is G, E, S, and K in a 2:1:1:3 molar ratio. a. Determine the sequence of the peptide? b. Determine the pl and position in an electrophoretic profile
A peptide with endorphin-like property was produced and obtained from the blood. This was sequence using the protocol: Treatment with streptococcal protease gave a tripeptide and a tetrapeptide. Treatment with trypsin gave two tripeptides and an amino acid. Treatment of the 2 tripeptide products in 1.2 with 2,4-dinitrophenol gave DNP- S, and DNP-E and a mixture of amino acids. The composition of the peptide is G, E, S, and K in a 2:1:1:3 molar ratio. What is the sequence of the peptide?
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.
Name the compound: 1. Lys-Ile-Met-Val Draw the forms of the amino acid in the solution. 2. Glutamic Acid (4 forms) 3. Lysine (4 forms)
A peptide was treated with Sanger's reagent followed by hydrolysis with 6M HCl for 24 hours at 105 oC. Chromatography of the mixture identified Val and Lys as the DNB labeled amino acids. Assuming a single peptide chain, explain how this could be and which is likely the actual N-terminal amino acid.
A NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare fungus. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrezine Nonapeptide Acid Hydrolysis (4 N HCI) at 110 C (2) Arg. Gin, (2) Tyr, Gly, Ser, Thr, and Met 2,4-dinitrolluorobenzene DNP-Thr Gin and Peptide 1 (Arg. Thr, Ser) modified free amino acids Cleavoge with Trypsin, then thrometography Peptide 2 (Gly, Tyr, Arg) Met Tripeptide (yenegen bromide Dipeptide Cleovoge with Chymetrypsin, then chromatography Peptide 3 (Arg, Ser, Tyr, Thr) Amino acid Peptide 4 (Gly, Arg, Tyr) When answering the questions below, please use the one-letter code for the amino acid, with NO spaces and symbols between each letter. 1. What is the N-terminal AA residue? 2. What is the C-terminal AA residue? 3. What is the sequence of Peptide 1? 4. What is the sequence of Peptide 4? 5. What is the overall amino acid…
A NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare fungus. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrazine Acid Hydrolysis (6 N HCI) at 110 "C Nonapeptide (2) Arg, Gln, (2) Tyr, Gly, Ser, Thr, and Met 2,4-dinitrofluorobenzene DNP-Thr Gin and modified free Peptide 1 (Arg, Thr, Ser) amino acids Cleavage with Trypsin, then chromatography Peptide 2 (Gly, Tyr, Arg) Met Tripeptide Cyanogen bromide Dipeptide Peptide 3 (Arg, Ser, Tyr, Thr) Cleavage with Chymotrypsin, then chromatography Amino acid Peptide 4 (Gly, Arg, Tyr)
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- 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.
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 decapeptide was analyzed and the following information obtained. Determine the primary structure of the peptide. Edman's Degradation: PTH-Ala Trypsin produces 3 peptides of the following composition: 1. Gly, His 2. Ala, Leu, Lys, Val 3. Arg (2), Phe, Pro Chymotrypsin produces 2 peptides of the following composition: 1. Ala, Leu, Lys, Phe, Val 2. Arg (2), Gly, His, Pro Elastase produces 1 amino acids and 3 peptides 1. Ala 2. Leu, Val 3. Arg (2), Lys, Phe, Pro, Gly, His Arg Gly His Leu Phe Pro Val
An amino acid mixture consisting of lysine,leucine, and glutamic acid is to be separated by ion-exchangechromatography, using a cation-exchange resin at pH 3.5, with theeluting buffer at the same pH. Which of these amino acids will beeluted from the column first? Will any other treatment be neededto elute one of these amino acids from the column?

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