Read very carefully: Chymotrypsin cleaves peptides C TERMINUS to thearomatic amino acids.Trypsin cleaves peptides C TERMINUS to basic amino acids.Cyanogen bromide (CNBR) cleaves C-terminus to methionine residues.With this knowledge, reconstruct the following cleavage products and givethe original peptide sequence.CNBRChymotrypsinWITHHERISALLRIGHTISTRYWITHMTrypsinEISAMYWITHMEISAMANINGCHEMISTRYWITHHER1Thewhichconvortede Name.

Trypsin and chymotrypsin are the proteases that break down protein into individual amino…

Answered: Read very carefully: Chymotrypsin…

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 15QP

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Consider the following peptide to answer the questions below: A M A K K E S H I F T A I D E What is the total charge of this peptide at pH = 5? What is the N terminal amino acid (full name)? C terminal amino acid? How many fragments would result if this peptide underwent proteolytic cleavage with V-8 protease and what are these fragments (list them)? Would this peptide be a candidate to form an alpha helix? Why or why not
The genetic code was deciphered by experiments in which synthetic polyribonucleotides of known repeating sequences were used as mRNAs to direct protein synthesis in cell - free extracts . What type or types of polypeptides would you expect to be synthesized if poly (AAG) n (A) AAGAAGAAG ) used as the template for in vitro peptide synthesis ?
Which amino acid residue is preferred at which position in the following peptide for cleavage by cyanogen bromide (CNBr)? methionine at R2 lysine at R1 methionine at R1 lysine at R2
The synthesis of a peptide is given by the mRNA sequence 5'GAAGAGAAACUUACU3', Find the primary structure of this peptide. If, due to a transcription error, the fourth, eighth, and ninth nucleotides are omitted, what peptide would be synthesized? Find the charge of each peptide at pH7 and explain whether this transcription error can affect the biological activity of said molecule.
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?
Use an arrow to draw the site for cleavage for the following peptides reacted by trypsin. Explain comprehensively.
Choose a pentapeptied composed of five different amino acids. List the five amino acids. Present the messenger RNA codons for the amino acids and the sequence of the nucleotids on the DNA that was originally coded for the pentapeptide.
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 FENYAT-2 ELIMVPKT-3 NFEEGSKT-4 ITGLAIHQKT-5 GSMDPVALMTLR C-1 DPVALMC-2 VPKGSMC-3 ITGLAIHQKELIMC-4 TLRNFEEGSKFENYA
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.
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.
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?

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