only items a-b Using an arrow, draw the site of cleavage for the following peptides that are reacted by: Pepsin (a-b), trypsin (c-d), and chymotrypsin (e).HHNPEPTIDE VPQFAGIa.HHb.PEPTIDE DLIPAE

Pepsin is a proteolytic enzyme made in the stomach that breaks down proteins in food during…

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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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Using an arrow, draw the site of cleavage for the following peptides that are reacted by trypsin
Use an arrow to draw the site for cleavage for the following peptides reacted by trypsin. Explain comprehensively.
You have isolated this peptide. AÇQGRKSPWTT TAHEVYPGGČMN What products would you get if you treated with: a) DTT ( dithiothreitol) b) Trypsin c) Carboxypeptidase A ( 1 cycle) d) Aminopeptidase M ( 2 cycles) e) DTT, then Iodoacetate, then elastase
Read very carefully: Chymotrypsin cleaves peptides C TERMINUS to the aromatic 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 give the original peptide sequence. CNBR Chymotrypsin WITHHERISALLRIGHT ISTRYWITHM Trypsin EISAM YWITHMEISAMANINGCHEMI STR YWITHHER 1 The which convorted e Name.
The first 32 amino acids from the N terminus of the protein bovine angiogenin were determined by Edman degradation and have the sequence:AQDDYRYIHFLTQHYDAKPKGRNDEYCFNMMK(a) Identify the sites of cleavage during trypsin-catalyzed hydrolysis of this protein.(b) What are the cleavage sites using chymotrypsin?
Consider the peptide Asp-Lys-Phe-Glu-Asn-Tyr-Gln-Val-Cys. In a single beaker, you treat this peptide with 2 proteases. One protease cleaves at the N-terminus of aromatic R groups and the other cleaves at the C-terminus of polar, non-ionizable R groups. Following the enzymatic digestion, you want to separate your peptide fragments so that you can identify them. You choose to separate the fragments using an anion exchange column. Beginning at pH=6 you apply your peptide fragments to the column and you gradually decrease the pH of the column stopping the separation when the pH of the column equals 4. Omitting chemical structures, write the amino acid sequence of the peptide fragments that are produced from this digest. Write the order that these fragments will elute from the column (if at all). (Relevant pKa values are: 2.1, 3.8, 4.3, 8.3, 9.6, 10.1, and 10.5)
A small protein has a sequence ACNCKAAPMLCARYCAMLH. The structure of this single peptide is stabilized by the formation of two separate disulfide bonds, but the locations of those disulfide bonds are unknown. In order to determine the location, you purify this peptide and treat it with trypsin (cleaves peptide bond at long, positively-charged side chains). Tryptic digestion generated two peptides. Based on this result, determine the location of the –S-S– bonds. Show them in a diagram on the sequence by connecting the corresponding residues. Explain your reasoning.
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?
Show the peptides that would result from cleavage by the indicated reagent: a. Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A b. Ser-Phe-Lys-Met-Pro-Ser-Ala-Asp by cyanogen bromide c. Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsin
H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14
A solution of peptide of unknown sequence was divided into 2 samples. One sample was treated with trypsin and the other one with pepsin. The fragments produced are given below: TRYPSIN A. Pro-Gly-Met-Phe-Leu-Arg B. Gln-Ile-Pro-Lys C. Ala-Gly-Trp-Lys PEPSIN A. Phe-Leu-Arg-Ala-Gly В. Pro-Gly-Met С. Тrр-Lys-Gln-Пе-Pro-Lys Deduce the original polypeptide chain.
Shown to the right is a cartoon image of ETC Complex I from Y. lipolytica. A group of authors studied this wild type Complex I and also a version where the arginine at position 121 in the chain 3 subunit was mutated to a methionine (R121M). Part of chain 3 subunit contains the peptide sequence SMITH a. Draw the titration curve for the SMITH peptide. Mark all pKa’s and the pI on your curve. For the SMITH peptide at physiological pH, explain what types of interactions you believe the side chains are or are not able to participate in.

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Using an arrow, draw the site of cleavage for the following peptides that are reacted by: Pepsin (a- b), trypsin (c-d), and chymotrypsin (e). H a. HN PEPTIDE VPQFAGI H b. PEPTIDE DLIPAE

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