Relative interfacial cleavage energetics of protein complexes revealed by surface collisions

Abstract

Significance There is a large gap between the number of protein complex structures currently solved and the number of functionally relevant structures. Mass spectrometry-based approaches for biomacromolecule structural characterization are growing, are beginning to fill critical gaps, and complement other structural biology tools. We have shown for several examples that collision of protein complex ions with a surface yields products that are reflective of substructure. We present here a computational model that predicts the relative appearance energy at which a globular protein complex dissociates. This appearance energy prediction can provide structural information when a high-resolution structure has not or cannot be obtained and in the future has potential to be used to select the best-fit candidate computational models, dramatically increasing the structural information obtained.