Trypsin, another member of the serine protease family has different substrate specificity, yet the same catalytic mechanism; it cleaves peptide bonds on the C side of arginine and lysine residues. What structural differences in the trypsin molecule bring about the changed substrate specificity?

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Tod ThielLv2

26 Sep 2018

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Trypsin, like other members of the serine protease family, contains in its active site three critical residues, referred to as the catalytic triad and shown in the figure at the right. In this drawing, the bonds between backbone atoms are shown in dark gray, and the side-chain bonds are light gray.Briefly but specifically, describe the role of each of these residues in the catalytic mechanism of a serine protease:

A) His 57

B) Ser 195

C) Asp 102

Please help explain the reagents and what they do, explain the reasoning behind the answers please, not simply the answer. I don't understand why the answers are what they are.:

The following reagents are often used in protein chemistry: CNBr, Urea, Mercaptoethanol, Chymotrypsin, Trypsin, Performic acid, 6N HCl, Pheyl isothiocyanate

Which one is the best suited for accomplishing each of the following tasks?

a) Determination of the amino acid sequence of a small peptide

b) Reversible denaturation of a protein devoid of disulfide bonds. Which additional reagent would you need if disulfide bonds were present?

c) Hydrolysis of peptide bonds on the carboxyl side of aromatic residues

d) Cleavage of peptide bonds on the carboxyl side of methionines

e) Hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues

Again, I know the answers are:

a) phenyl isothiocyanate b) urea and Î²-mercaptoethanol to reduce disulfides c) chymotrypsin d) CNBr e) trypsin

However, I have no idea why they are the correct answers. Thank you.

skyyellowjacket162

1. tRNA aminoacylation

a. What is aminoacylation? Where on the tRNA does it occur?

b. Why is ATP required for aminoacylation? Why is the hydrolysis of PPi generated during aminoacylation important?

c. What is the significance of the high-transfer potential of the ester bond created during tRNA aminoacylation?

d. Why is the specificity of aminoacyl-tRNA synthetases important? How do these enzymes ensure their specificity?

e. Are you familiar enough with amino acid side chains to answer questions about aminoacyl-tRNA synthetase specificity? (e.g. how might similar amino acids like valine, serine and threonine be distinguished?)

f. Do you understand why there are differences in amino acid recognition between activation and editing sites? And how those differences dictate the specificity of the two different activities?