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- W2158162199 abstract "Cysteine is a significant amino acid residue in that it can form a disulfide bridge with another cysteine (to form cystine). Such disulfide bridges are important determinants of protein structure. No known endoproteinase shows specificity solely for cysteinyl, or cystinyl, residues, although endoproteinase Asp-N is able to hydrolyze bonds to the amino-(N)-terminal side of aspartyl or cysteinyl residues. Modification of aspartyl residues (1) can generate specificity for cystei-nyl residues. Again, as discussed by Aitken (2), modification of cysteinyl to 2-aminoethylcysteinyl residues makes the bond to the carboxy-(C)-terminal side susceptible to cleavage by trypsin, or the bond to the N-terminal side sensitive to Lys-N. However, specific cleavage of bonds to the N-terminal side of cysteinyl residues may be achieved in good yield by chemical means [(3); see Note 1]. The cleavage generates a peptide blocked at its N-terminus as the cysteinyl residue is converted to an iminothiazolidinyl residue, but peptide sequencing can be carried out after conversion of this residue to an alanyl residue (4). Cysteine is one of the less frequent amino acids in proteins, and cleavage at cysteinyl residues tends to generate relatively large peptides. Thus, the method described in this chapter has been used to generate separate domains of troponin C for the purpose of studying Ca and peptide binding (5), and peptides from vinculin to study talin- and anti-vinculin antibody binding (6). It has also been adapted for the purposes of “footprinting”: Cys residues that remain protected in a native protein remain noncyanylated on reaction with 2-nitro-5-thiocyanoben-zoate, and remain uncleaved upon alteration of the pH to 9.0. Thus the protected Cys residues can be mapped within the proteins sequence (7)." @default.
- W2158162199 created "2016-06-24" @default.
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- W2158162199 date "2009-01-01" @default.
- W2158162199 modified "2023-09-23" @default.
- W2158162199 title "Chemical Cleavage of Proteins at Cysteinyl-X Peptide Bonds" @default.
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- W2158162199 doi "https://doi.org/10.1007/978-1-59745-198-7_97" @default.
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