Which of these reagents is commonly used to determine the number of polypeptides in a protein? O iodoacetate O dansyl chloride O 2-mercaptoethanol (B-ME) O cyanogen bromide O DEAE
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Valuable reagents often used in protein chemistry are: Trypsin, Ninhydrin, CNBr, Phenyl isothiocyanate, Urea, Performic acid, 6 N HCl, Chymotrypsin, and Mercaptoethanol. 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.
Adi S.
The ionic charges associated with protein molecules are mostly contributed by the side chains of constituent amino acids. This is determined by the Α-carboxyl group, Α-amino group, and side chain of each amino acid. The charges contributed by the N-terminal and C-terminal residues are independent of the amino acid composition and depend only on pH. The number of disulfide bonds also plays a role in determining the charges. Which substance is used to fractionate proteins based on differences in their solubility as a function of salt concentration? A. Coomassie blue B. Ammonium sulfate C. Dialysis membrane D. Phenylisothiocyanate E. Sodium dodecyl sulfate Gel-filtration chromatography separates mixtures of proteins based on their size, density, tendency to form aggregates, and binding affinity of the protein for the column matrix. Which reagent will react with amino acids to yield derivatives that can be detected by monitoring the absorbance of UV light? A. PITC B. SDS C. CNBr D. HCl E. Β-mercaptoethanol
Josee P.
The following reagents are often used in protein chemistry. Match the reagent with the purpose for which it is best suited. Some answers may be used more than once or not at all; more than one reagent may be suitable for a given purpose. Place letter(s) next to each purpose. (a) cyanogen bromide (b) performic acid (c) phenylisothiocyanate (d) chymotrypsin (e) FDNB (f) trypsin (g) dithiothreitol 1. Hydrolysis of peptide bonds on the carboxyl side of Lys and Arg 2. Cleavage of peptide bonds on the carboxyl side of Met 3. Breakage of disulfide (S-S) bonds 4. Determination of the amino acid sequence of a peptide 5. Determining the amino-terminal amino acid in a polypeptide
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