______ 1. is a serine protease that cuts the peptide after aromatic amino acids ______ 2. is a type of chemical bond formed by chymotrypsin with its substrate as a first step in the reaction mechanism ______ 3. is the name of the compound that hydrolyzes the chemical bond formed between chymotrypsin and its substrate ______ 1. is the name of the inactive form of chymotrypsin

1. is a serine protease that cuts the peptide after aromatic amino acids 2. is a type of chemical bond formed by chymotrypsin with its substrate as a first step in the reaction mechanism 3. is the name of the compound that hydrolyzes the chemical bond formed between chymotrypsin and its substrate 1. is the name of the inactive form of chymotrypsin

BIOLOGY:CONCEPTS+APPL.(LOOSELEAF)

10th Edition

ISBN:9781305967359

Author:STARR

Publisher:STARR

Chapter3: Molecules Of Life

Section: Chapter Questions

Problem 13SA

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Similar questions

From the oligopeptide below, write completely the amino acids and/or peptide fragments that resulted from the reaction of trypsin. The amino acids and residues should be represented by the three-letter abbreviation.
What is the name of the prosthetic group in the image , In the left image the prosthetic group is covalently linked to the enzyme. what is the nature of the bond.and in which step of the reacion is the prosthetic group covalentlylinked to the protein?image on the right what step in the reaction is depicted and what else needs to happen to complete this part of the reaction?
Illustrate the pathways to synthesize the following aminoacids:a. glutamineb. serinec. arginined. glycinee. cysteine
The dynorphins are a group of opioid peptides that play an important role in changes in the brain associated with cocaine addiction. One of these peptides, dynorphin A, contains the following amino acid sequence: Tyr–Gly–Gly–Phe–Leu–Arg–Arg–Ile–Arg–Pro–Lys–Leu–Lys. Draw the amino acids and peptide fragments formed when dynorphin A is treated with each reagent or enzyme: (a) chymotrypsin; (b) trypsin; (c) carboxypeptidase; (d) C6H5N=C=S.
Proteins treated with proteolytic enzymes hydrolyzed peptide bonds to yield a mixture of amino acids only. Is the statement TRUE OR FALSE?
Draw the structure of the following: (in the image provided)Use the amino acids below.F - PhenylalanineI - IsoleucineG - GlycineH - HistidineT - ThreonineE - Glutamic acidR - Arginine
A drug company has decided to use recombinant DNA methods to prepare a modified α1 -antitrypsin that will be more resistant to oxidation than is the naturally occurring inhibitor. Which single amino acid substitution would you recommend?
A drug company has decided to use recombinant DNA methods to prepare a modified α 1 - antitrypsin that will be more resistant to oxidation than is the naturally occurring inhibitor. Which single amino acid substitution would you recommend?
From the oligopeptide below, write completely the amino acids and/or peptide fragments that resulted from the reaction of elastase. The amino acids and residues should be represented by the three-letter abbreviation.
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?
In the deoxy state, Histidine forms an ______ salt bridge with aspartate and an ______ salt bridge with lysine in the deoxidized state. a) Intra-chain; Intra-chain b) Intra-chain; inter-chain c) Inter-chain; Inter-chain d) Inter-chain; Intra-chain
Determine the amino acid sequence of a polypeptide from the following data:Complete hydrolysis of the peptide yields Arg, 2 Gly, Ile, 3 Leu, 2 Lys, 2 Met, 2 Phe, Pro, Ser, 2 Tyr, and Val.Treatment with Edman’s reagent releases PTH-Gly.Carboxypeptidase A releases Phe. Treatment with trypsin yields the following four peptides:1. Gly-Leu-Tyr-Phe-Lys 3. Val-Ile-Arg2. Ser-Met-Gly-Leu-Tyr-Lys 4. Met-Leu-Pro-Phe