An integrated chemical cross-linking and mass spectrometry approach to study protein complex architecture and function.

ABSTRACT: Knowledge of protein structures and protein-protein interactions is essential for understanding biological processes. Chemical cross-linking combined with mass spectrometry is an attractive approach for studying protein-protein interactions and protein structure, but to date its use has been limited largely by low yields of informative cross-links (because of inefficient cross-linking reactions) and by the difficulty of confidently identifying the sequences of cross-linked peptide pairs from their fragmentation spectra. Here we present an approach based on a new MS labile cross-linking reagent, BDRG (biotin-aspartate-Rink-glycine), which addresses these issues. BDRG incorporates a biotin handle (for enrichment of cross-linked peptides prior to MS analysis), two pentafluorophenyl ester grou

SUBMITTER: Luo J 

PROVIDER: S-EPMC3277749 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature