i need help with 1. The following reagents are often used in protein chemistry:

Question

i need help with 1.

The following reagents are often used in protein chemistry: CNBr Trypsin Urea Mercaptoethanol Chymotrypsin Trypsin Performic acid 6 N HCI Phenyl 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. The only constant is change. Explain how two different cell types from the same organism will have identical genomes but may have vastly divergent proteomes. Crafting a new breakpoint. Ethyleneimine reacts with cysteine side chains in proteins to form S-aminoethyl derivatives. The peptide bonds on the ca

Explanation / Answer

a) Determination of aminoacid sequence of a small peptide - phenyl isothiocyanate

b) Reversible denaturation of protein devoid of disulfide bonds. Which additional reagent would you need if disulfide bonds are present? - urea and  -mercaptoethanol to reduce disulfides

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

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

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

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