Finally, the researcher incubates the peptide with chymotrypsin for two hours at 10 °C and analyzes the products usingchromatography. Complete chymotryptic digestion of the peptide with chymotrypsin followed by chromatography yields freetyrosine and free leucine, plus a tripeptide containing Phe and Gly in a 1:2 ratio.Give the final sequence for the peptide based on the results of the acid hydrolysis, dansyl chloride reaction, and chymotrypticdigestion. Use the three-letter amino acid abbreviations separated by hyphens for your answer.peptide sequence:

Peptide digestion refers to the process of breakdown of peptide primary structure for different…

Answered: Finally, the researcher incubates the…

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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Similar questions

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. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain
The sequence of a peptide is given below. YGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE If you perform peptide sequencing by tandem mass spectroscopy, calculate the predicted m/z ratio for b1, b5, b12, y1, y5 and y12 ions.
The OXA-M290 protein is next purified by size exclusion chromatography. To determine the best type of size exclusion resin to use, the size of OXA-M290 must first be determined. Earlier, you determined the amino acid sequence of OXA-M290 (MRVLALSAVFLVASIIGMPAVAKEWQENKSWNAHFTEHKSQGVVVLWNENKQQGFTNNLKRANQAFLPASSAKIPNSLIALDLGVVKDEHQVFKWDGQTRDIATWNRDHNLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNEDISGNVDSFWLDGGIRISATEQISFLRKLYHNKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYDTKIGWWVGWVELDDNVWFFAMNMDMPTSDGLGLRQAITKEVLKQEKIIP). Based on the amino acid sequence, what is the molecular weight of this protein? You can use the free ProtParam tool (https://web.expasy.org/protparam/) to calculate the molecular weights of proteins. Make sure to include units in your answer. Note: The amino acid sequence reported earlier does not include the His-tag that was added to OXA-M290 by the pET-28a vector. However, you do not need to consider the amino acids in the His-tag in your answer to this question. For Context ONLY: For…
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
Peptide Y is a polymorphic analogue of Peptide X. If peptide X with endorphin-like property was produced and obtained from the blood and was sequenced 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. Sanger products using ddGTP Mononucleotide Decanucleotide Trinucleotide 12-nucleotide Tetranucleotide 13-nucleotide Pentanucleotide 14-nucleotide Hexanucleotide 16-nucleotide nonanucleotide 21-nucleotide a. Using the table with the following Sanger products using ddGTP, what is the unique base sequence of the template DNA coding for the polymorphic peptide sequence? b. Peptide X is N-linked to a saccharide, with which amino acid in Peptide X is the saccharide linked? Also show the…
Predict the amino acid sequence based on the conditions below. Use the one-letter abbreviation of amino acids. a. The amino acid in the C-terminal is optically inactive. b. The fifth amino acid is a neutral aromatic amino acid that yields a negative result for the Xanthoproteic test using intact protein while producing a yellow soln with Xanthoproteic reagent and yielding a negative result with Hopkin's Cole test using basic hydrolysate. c. Yields serine and a hexapeptide after treatment of aminopeptidase (specificity: peptide bond on the N-terminus). d. The amino acid beside the N-terminal a.a. will yield ornithine and urea after alkaline hydrolysis. e. The third amino acid gives a positive result for Hopkins-Cole Test. f. Chymotrypsin cannot cleave the peptide bond on the fifth amino acid because of the presence of this a.a. residue. g. The amino acid at the carboxy-end of the third a.a. will yield a black precipitate for Pb(Ac)2.
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 the native peptide was exposed to cyanogen bromide (CNBr), an octapeptide and free glycine were recovered. Incubation of the native peptide with trypsin gave a pentapeptide, a tripeptide, and free Lys. 2,4-Dinitrophenyl-histidine was recovered from the pentapeptide, and 2,4-dinitrophenylphenylalanine was recovered from the tripeptide. Digestion with the enzyme pepsin produced a dipeptide, a tripeptide, and a tetrapeptide. The tetrapeptide was composed of (Lys) 2, Phe, and Gly. The native sequence was determined to be: Met-Leu-Phe-Lys-Phe-Gly-Gly-Lys-His His-Leu-Gly-Lys-Lys-Phe-Phe-Gly-Met His-Phe-Leu-Gly-Lys-Lys-Phe-Met-Gly Gly-Phe-Lys-Lys-Gly-Leu-Met-Phe-His ● His-Leu-Phe-Gly-Lys-Lys-Phe-Met-Gly
A tridecapeptide yields the following fragments when partially hydrolized. Determine the sequence of amino acids in the tridecapeptidedrolyzed. Determine the sequence of the tri decapeptide. tridecapeptide à lys-arg + gly-phe-pro + phe-ser-asp-lys + pro-phe-ser + asp-lys-arg-val + gln-ala-tyr + val-trp-gln. Determine the sequence of amino acids in the tridecapeptide
Predict the amino acid sequence based on the conditions below. Use the one-letter abbreviation of amino acids. ___1___--_2_- 3 -- --____6_--_7__ a. The amino acid in the C-terminal is optically inactive. b. The fifth amino acid is a neutral aromatic amino acid that yields a negative result for the Xanthoproteic test using intact protein but produces a yellow soln with basic hydrolysate. It also gives a negative result with both Hopkin's Cole and Millon's test using basic hydrolysate. c. After treatment of this peptide with aminopeptidase (specificity: peptide bond on the N-terminus), it yields serine and a hexapeptide d. The amino acid besides the N-terminal amino acid. will yield ornithine and urea after alkaline hydrolysis. e. The third amino acid gives a positive result for Hopkins-Cole Test. f. Chymotrypsin^ cannot cleave the peptide bond on the fifth amino acid because of the presence of this a.a. residue. g. The amino acid at the carboxy-end of the third amino acid will yield a…
A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin, and the other with cyanogen bromide. Given the following sequences of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment: Asn-Thr-Trp-Met-Ile-Lys Gly-Tyr-Met-Gln-Phe Val-Leu-Gly-Met-Ser-Arg Cyanogen Bromide treatment: Gln-Phe Ile-Lys-Gly-Tyr-Met Ser-Arg-Asn-Thr-Trp-Met

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