Mass spectrometry studies of protein folding

Abstract

Mass spectrometry has become a powerful method to study the structure and dynamics of proteins. Hydrogen/deuterium exchange in conjunction with mass spectrometry is now becoming more widely used to monitor conformational changes in proteins, and when combined with proteolytic digestion or gas-phase dissociation, it can provide spatial resolution of structural regions which participate in conformational change. The biggest advantage offered by mass spectrometry is that it can distinguish different conformations of a protein even when they are present together, and this has made it an indispensable tool for studying the heterogeneity inherent in protein folding and unfolding reactions. This review surveys the application of mass spectrometry to study protein folding and unfolding reactions, and describes the important insights obtained from these studies. Its also briefly examines the use of mass spectrometry to study the assembly and disassembly of large multimeric protein complexes, and to obtain structural information on amyloid protofibrils and fibrils.