Protein footprinting in a complex milieu: identifying the interaction surfaces of the chemotaxis adaptor protein CheW.

ABSTRACT: Characterizing protein-protein interactions in a biologically relevant context is important for understanding the mechanisms of signal transduction. Most signal transduction systems are membrane associated and consist of large multiprotein complexes that undergo rapid reorganization--circumstances that present challenges to traditional structure determination methods. To study protein-protein interactions in a biologically relevant complex milieu, we employed a protein footprinting strategy based on isotope-coded affinity tag (ICAT) reagents. ICAT reagents are valuable tools for proteomics. Here, we show their utility in an alternative application--they are ideal for protein footprinting in complex backgrounds because the affinity tag moiety allows for enrichment of alkylated species prior

SUBMITTER: Underbakke ES 

PROVIDER: S-EPMC3179904 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature