TPCK is a molecule with large hydrophobic groups.Why does TPCK inactivate chymotrypsin but not trypsin?TPCK looks like the substrate for chymotrypsin, but not trypsin, and thus can bind in its active site and modify His-57.Trypsin does not have a His residue present in the active site to react with TPCK.TPCK is a transition state analog for chymotrypsin, but not trypsin.TPCK binds to trypsin but does not modify its active site.

Proteases are enzymes responsible for cleaving peptide bonds. Chymotrypsin and trypsin are both…

Answered: TPCK is a molecule with large…

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

Catalytic residues are often found in loops between helices or strands for increased mobility duringcatalysis. Is the catalytic Cys predicted to be located in a loop between helices/strands?Are the other two catalytic residues, His and Asn, also found in loops?
Which of the following sequences represents a recognition site for N-linked glycosylation where X is any amino acid residue? Gln-X-Ser O His-X-Ser O Arg-X-Ser O Asn-X-Ser O Asp-X-Ser
What's the simple rule to predict ligand binding sites for Rossmann Fold
What is the first thing that must occur in order for the catalysis of the peptide bond to begin. What is a specificity pocket? What are the preferences of chymotrypsin due to its specificity pocket?
(c) On the right is a diagram of the ac tive site of E. coli aspartate aminotrans- ferase illustrating the cofactor pyridoxal phosphate (labeled PLP) with the dicar- boxylic acid maleate (labeled MAL) bound in the active site. The structural formula of maleate is shown on the right. Am 194 MAL Arg292 Arg386 Ilx17 Lauf 'coo- H get H Coo- Maleate (c1) Draw the structure of L-aspartate and draw a border around the atoms in the amino acid that maleate simulates. (c2) Identify the active site residues that make hydrogen bonds and electrostatic interac- tions with the oxygen atoms of the carboxylate groups of maleate in the diagram above. Identify the carboxylate groups according to the numbering in the diagram of maleate above. Indicate the hydrogen donor groups of the active site residues. (C3) Compare and draw the structures of L-Arg and L-Lys. On the basis of the diagram why does replacement of an arginine for a lysine have an effect on substrate binding to AspAT? (c4) Of the mutant…
TLCK and TPCK both use Histadine residues in the active site as inhibitors of serine proteases. Why is TLCK specific for trypsin and TPCK is specific for chymotrypsin?
There are around 20 different versions of this molecule, which create different proteins when linked up in different sequences (like different letters making different words). What is one of these linked molecules named? * GLN ASP MET LEU MET SER LYS ASP GLU HIS THR LEU ILE LEU TRP LYS GLY GLN PRO PRO THR GLY: Glycine TRP: Tryptophan HIS: Histidine MET: Methionine THR: Threonine ASP: Aspartic acid LYS: Lysine ILE: Isoleucine LEU: Leucine GLU: Glutamic acid ALA: Alanine PRO: Proline SER: Serine GLN: Glutamine O Carbohydrate O Amino Acid O Nucleotide O Lipid
An engineered ligand binds its target with 5 nM affinity at high pH. However, protonation of a histidine residue in the binding site of the ligand renders it unable to bind. Plot the ligand:target complex concentration versus the initial ligand concentration (in protonated or unprotonated form) at pH 4, 5, 6, 7, or 8 (five lines on one plot). Use a total target concentration of 10 nM.
The catalytic triad consists of Asp, His, and Ser. What would be an alternative for histidine and how would we draw the interactions in a mechanism?
Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…
What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine? In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?
Can you please describe the specific components that each of these structures are comprised of ( alpha helices and beta sheets) in more detail? Also, what do the different colors represent? Your reply will be greatly appreciated. The ligand that was assigned to me is tadalafil.

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