Characterization of disulfide bonds by planned digestion and tandem mass spectrometry.

ABSTRACT: The identification of disulfide bonds provides critical information regarding the structure and function of a protein and is a key aspect in understanding signaling cascades in biological systems. Recent proteomic approaches using digestion enzymes have facilitated the characterization of disulfide-bonds and/or oxidized products from cysteine residues, although these methods have limitations in the application of MS/MS. For example, protein digestion to obtain the native form of disulfide bonds results in short lengths of amino acids, which can cause ambiguous MS/MS analysis due to false positive identifications. In this study we propose a new approach, termed planned digestion, to obtain sufficient amino acid lengths after cleavage for proteomic approaches. Application of the DBond softwa

SUBMITTER: Na S 

PROVIDER: S-EPMC4410109 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature