Relative interfacial cleavage energetics of protein complexes revealed by surface collisions.

ABSTRACT: To fulfill their biological functions, proteins must interact with their specific binding partners and often function as large assemblies composed of multiple proteins or proteins plus other biomolecules. Structural characterization of these complexes, including identification of all binding partners, their relative binding affinities, and complex topology, is integral for understanding function. Understanding how proteins assemble and how subunits in a complex interact is a cornerstone of structural biology. Here we report a native mass spectrometry (MS)-based method to characterize subunit interactions in globular protein complexes. We demonstrate that dissociation of protein complexes by surface collisions, at the lower end of the typical surface-induced dissociation (SID) collision ene

SUBMITTER: Harvey SR 

PROVIDER: S-EPMC6486728 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature