Determinants of gas-phase disassembly behavior in homodimeric protein complexes with related yet divergent structures.

ABSTRACT: The overall structure of a protein-protein complex reflects an intricate arrangement of noncovalent interactions. Whereas intramolecular interactions confer secondary and tertiary structure to individual subunits, intermolecular interactions lead to quaternary structure--the ordered aggregation of separate polypeptide chains into multisubunit assemblies. The specific ensemble of noncovalent contacts dictates the stability of subunit folds, enforces protein-protein binding specificity, and determines multimer stability. Consequently, noncovalent architecture is likely to play a role in the gas-phase dissociation of these assemblies during tandem mass spectrometry (MS/MS). To further advance the applicability of MS/MS to analytical problems in structural biology, a better understanding of th

SUBMITTER: Dodds ED 

PROVIDER: S-EPMC3094495 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature