A polypeptide is cleaved into peptides by treatment with trypsin and cyanogen bromide, and then the peptides are purified and sequenced. The sequences of the peptides are shown below. Trypsin peptides Cyanogen bromide peptides Based on sequences of the overlapping peptides generated by treatment with trypsin and cyanogen bromide (shown above), which of the following peptides represents the N-terminus of the original polypeptide? A. T-1 B. T-4 C. C-2 D. C-4 T-1 FENYA T-2 ELIMVPK T-3 NFEEGSK T-4 ITGLAIHQK T-5 GSMDPVALMTLR C-1 DPVALM C-2 VPKGSM C-3 ITGLAIHQKELIM C-4 TLRNFEEGSKFENYA

A polypeptide is cleaved into peptides by treatment with trypsin and cyanogen bromide, and then the peptides are purified and sequenced. The sequences of the peptides are shown below. Trypsin peptides Cyanogen bromide peptides Based on sequences of the overlapping peptides generated by treatment with trypsin and cyanogen bromide (shown above), which of the following peptides represents the N-terminus of the original polypeptide? A. T-1 B. T-4 C. C-2 D. C-4 T-1 FENYA T-2 ELIMVPK T-3 NFEEGSK T-4 ITGLAIHQK T-5 GSMDPVALMTLR C-1 DPVALM C-2 VPKGSM C-3 ITGLAIHQKELIM C-4 TLRNFEEGSKFENYA

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 18QP: The following is a portion of a protein: met-trp-tyr-arg-gly-pro-thr-Various mutant forms of this...

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Digestion of a peptide with trypsin generates two smaller peptide products: methionine-glycine and tyrosine-lysine. Digestion of the same peptide with cyanogen bromide (CNBr) also generates two smaller peptide products: glycine and tyrosine-lysine-methionine. What is the sequence of the original peptide? a.) tyrosine-lysine-methionine-glycine b.) methionine-glycine-tyrosine-lysine c.) glycine-tyrosine-lysine-methionine d.) tyrosine-glycine-methionine-lysine
A sample of a peptide of unknown sequencewas treated with trypsin; another sample of the same peptide wastreated with chymotrypsin. The sequences (N-terminal to C-terminal)of the smaller peptides produced by trypsin digestion were as follows:
Based on the following image, what is the N-terminal AA residue, C-terminal AA residue? What is also the sequence of peptide 2 and peptide 3? Also identify the overall amino acid sequence
A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin and the other was treated with cyanogen bromide. Given the following sequences (N-terminal to C-terminal) of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment Asn—Tyr—Asp—Met—Phe—Ala—Arg Asp—Trp—Asn—Arg Gln—Met—Tyr—Cys—Pro—Ile—Arg Gln—Cys Cyanogen bromide treatment Tyr—Cys—Pro—Ile—Arg—Asn—Tyr—Asp—Met Asp—Trp—Asn—Arg—Gln—Met Phe—Ala—Arg—Gln—Cys
A heptapeptide when treated with trypsin produced two peptides. T1 (D, G, Y) and T2 (K, F, V, A). When the heptapeptide was treated with chymotrypsin, three peptides were produced: CT1 (K,,Y, G), CT2 (F,A, V), and CT3 (D). The sequences of these peptides is not known, however. When the peptide was treated with Sanger’s Reagent and hydrolyzed, DNP-K and DNP-A were recovered. What is the amino acid sequence of the heptapeptide?
Shown below is a portion of a DNA sequence ( 31 base pairs long ) that encodes the last amino acids of a protein : The first three underlined base pairs indicate the frame and include the coding region . 123456789 A. Write the peptide sequence of the last 6 amino acids of the protein . Label both ends of the peptide . B. A insertion of one base pair causes the protein to decrease in length by 5 amino acids . With respect to the sequence given above , where does this insertion occur , and what base pair will you insert ? C. An change of one base pair leads to the protein to increase in length by one amino acid. With respect to the sequence given above , which base pair would you change ? How would you change this base pair for the protein to increase in length by one amino acid ?
A peptide has the following amino acid composition: 2 Met, 2 Phe, 2 Glu, 1 Arg, 1 Lys, 1 Val, 1 Leu, 1 Gly, 1 Ser Reaction of the intact peptide with dansyl chloride followed by acid hydrolysis creates a derivative of Met. A specific cleavage of the intact peptide produces fragments with the following sequences: Fragment A: Glu-Gly-Lys-Phe Fragment B: Met-Ser-Leu-Arg Fragment C: Met-Val-Glu-Phe Which reagent was used for the specific cleavage? Cyanogen bromide Carboxypeptidase A Trypsin Chymotrypsin
A peptide has the following amino acid composition: 2 Met, 2 Phe, 2 Glu, 1 Arg, 1 Lys, 1 Val, 1 Leu, 1 Gly, 1 Ser Reaction of the intact peptide with dansyl chloride followed by acid hydrolysis creates a derivative of Met. A specific cleavage of the intact peptide produces fragments with the following sequences: Fragment A: Glu-Gly-Lys-Phe Fragment B: Met-Ser-Leu-Arg Fragment C: Met-Val-Glu-Phe What information do this result give about the sequence of the peptide? Explain how you arrived on you answer.
How many different sequences of mRNA could encode a peptide with the sequence proline-glycine-methionine-serine?
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
How do you think incorporating a-methylserine into a peptide would affect the structure and/or polarity of the peptide compared to a serine residue?
The following steps were performed using enzyme cleavage of a peptide to determine its amino acid sequence. Step 1. FDNB yield DNB-Gly Step 2. Treatment with trypsin yield 3 fragments: Tyr-Leu-Asp-Arg; Gly-Ser-Ala-Lys; Trp-Gly-Ser-Met Step 3. Treatment with pepsin gave the same 3 peptide fragments. What is the sequence of the peptide?