A key factor in varied protein functionality is their ability to self-assemble and interact with one another to create vast molecular machines, capable of performing intricate cellular tasks. Because of their importance in biology, multiprotein complexes are amongst the most important drug targets, but in many cases we lack the analytical tools necessary to characterize small molecule interactions within such protein assemblies.   Over the past several years, we have been building nano-electrospray ionization (nESI) coupled to ion mobility-mass spectrometry (IM-MS) into a tool capable of characterizing multiprotein-ligand complexes from mixtures, using microgram amounts of protein and without requiring covalent labels or tagging.  Our main approach is the collision induced unfolding (CIU) of proteins and complexes, which functions as a highly sensitive and selective analog of solution-based calorimetry experiments for gas-phase proteins.  This presentation will discuss our most-recent CIU datasets, and illustrate the utility of this tool in structural biology.

Collision induced unfolding: From novel protein stability measurements to high-throughput ligand screening

245th National Meeting (2013)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.