Deduce the amino acid sequence of a polypeptide from the following: 1. Acid hydrolysis gives Ala2, Arg, Lys2, Met, Phe, Ser2 2. Carboxypeptidase gives Ala 3. Trypsin digestion gives 4 peptides a) Ala, Arg b) Lys, Phe, Ser c) Lys d) Ala, Met, Ser 4. CNBr treatment gives a) Ala, Arg, Lys2, homoserine, Phe, Ser b) Ala, Ser 5. Thermolysin is a protease that cuts on the N-terminal side of hydrophobic amino acids (substrate preference is Leu, Ile, Phe, Trp, Tyr, Val). Thermolysin treatment of our polypeptide yields 2 peptides a) Ala, Arg, Ser b) Ala, Lys2, Met, Phe, Ser
Deduce the amino acid sequence of a polypeptide from the following:
1. Acid hydrolysis gives Ala2, Arg, Lys2, Met, Phe, Ser2
2. Carboxypeptidase gives Ala
3. Trypsin digestion gives 4 peptides
a) Ala, Arg
b) Lys, Phe, Ser
c) Lys
d) Ala, Met, Ser
4. CNBr treatment gives
a) Ala, Arg, Lys2, homoserine, Phe, Ser
b) Ala, Ser
5. Thermolysin is a protease that cuts on the N-terminal side of hydrophobic amino acids (substrate preference is Leu, Ile, Phe, Trp, Tyr, Val). Thermolysin treatment of our polypeptide yields 2 peptides
a) Ala, Arg, Ser
b) Ala, Lys2, Met, Phe, Ser
Deducing the amino acid sequence of a polypeptide from the analysis of peptide fragments generated from enzymatic cleavage involves a series of steps to identify the bond cleavage sites and the resulting peptide fragments.
These fragments can then be used to reconstruct the original peptide sequence based on the location and identity of the amino acids in each fragment. By combining information from multiple cleavage reactions, it is possible to deduce the complete amino acid sequence of the original peptide.
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