The trypsin enzyme is able to hydrolyze a peptide substate at the carboxylside of an Arg or Lys residue. However, such a reaction can be alsoinfluenced by the amino acid residue that follows Arg or Lys. Given theMichaelis-Menton plots obtained for two substrates (substrate A: Ser-Val-Arg-Pro; substrate B: Ser-Val-Arg-Phe), the Km of the enzyme is higherfor:20Substrate AAssumethat thesecurves donot reachthe samelimit.15Substrate E0.0010.0020.003(Substrate) (molar)InconclusiveSubstrate BBoth Substrate A and BIntitial velocity(micromoles/literisecond)

Enzymes are protein molecules that increase the rate of enzyme reactions by decreasing the…

Answered: The trypsin enzyme is able to hydrolyze…

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

Some of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.
Given the following pKa data for the individual amino acids, estimate the pI for the tripeptide Thr-Asp-Arg. N-terminal amino group = 9.10 Side chain of aa #1 = Side chain of aa # 2 = 3.86 Side chain of aa # 3 = 12.48 C-terminal carboxyl group = 2.01 PI =
Similarly, hypoxanthine (HX) can be used to label purine residues. As in Problem 4, write reactions showing the conversion of hypoxanthine to dATP and dGTP.
A tetrapeptide, glutamate-glycine-alanine-lysine, is prepared at at concentration of 1 mM (0.001 M) and is measured in the standard setup (pathlength of 1 cm). What is the approximate absorbance of this peptide at 280 nm? Hint: if the peptide contained a single tryptophan, the answer would be about 10. 10 280 1 0
Heparin, a highly negatively charged glycosaminoglycan, is used clinically as an anticoagulant. It acts by binding several plasma proteins, including antithrombin III, an inhibitor of blood clotting. The 1:1 binding of heparin to antithrombin III seems to cause a conformational change in the protein thatgreatly increases its ability to inhibit clotting. What amino acid residues of antithrombin III are likely to interact with heparin?
A binding curve for the binding of the amino acid tryptophan to the protein called TxtE is shown below. Estimate the association equilibrium constant (Ka; in units of M-1) for Trp binding to TxtE.
A peptide with the primary structure Lys-Arg-Pro-Leu-Ile-Asp-Gly-Ala must be synthesized by the methods developed by Merrifield. Calculate the percentage of the peptides synthesized that will be full length and have the correct sequence if the addition of each amino acid residue is 96% efficient. Do the calculation a second time but assume a 99% efficiency for each cycle. full-length peptides with the correct sequence if 96% efficient: full-length peptides with the correct sequence if 99% efficient: % %
you have the following peptide Arg-Ile-Pro-Leu-Asp-Lys-Glu The net charge on this peptide at pH 7.0 is ?. The net charge on this peptide at 1M HCl is ?.
Please provide a separation solution of combining two types of chromatography to isolate the protein A from the mixture containing protein A, B, C and D (shown as below). And then explain the related mechanisms in details. Protein A: Met-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu- Protein B: Met-Asp-Glu-Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu Protein C: Met-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu-Val-Val-Val- Ile-lle-lle-Leu-Leu- Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle- lle-Leu-Leu-Leu-Leu-Val-Val-Val-Ile- Protein D: Met-Asp-Glu--Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu-Glu-Asp- Glu-Asp-Glu-Glu-Asp-Asp-Glu-Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu-Glu- Asp-Glu-Asp-Glu-Glu-Asp-Glu-Glu-Asp
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?
Determine the pI of the peptide H2N-Ala-Lys-Ser-Arg-COOH at pH 11, please explain why some pKas are used in the solution of the problem while others are not.
The hydrolysis of a phenylalanine-containing peptide is catalyzed by a-chymotrypsin with the following results. Calculate KM and Vmax for the reaction. What is the equation of the line?

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