Development of a novel cross-linking strategy for fast and accurate identification of cross-linked peptides of protein complexes.

ABSTRACT: Knowledge of elaborate structures of protein complexes is fundamental for understanding their functions and regulations. Although cross-linking coupled with mass spectrometry (MS) has been presented as a feasible strategy for structural elucidation of large multisubunit protein complexes, this method has proven challenging because of technical difficulties in unambiguous identification of cross-linked peptides and determination of cross-linked sites by MS analysis. In this work, we developed a novel cross-linking strategy using a newly designed MS-cleavable cross-linker, disuccinimidyl sulfoxide (DSSO). DSSO contains two symmetric collision-induced dissociation (CID)-cleavable sites that allow effective identification of DSSO-cross-linked peptides based on their distinct fragmentation patt

SUBMITTER: Kao A 

PROVIDER: S-EPMC3013449 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature