Understanding protein dynamics using conformational ensembles

Abstract

Conformational ensembles are powerful tools to represent the range of conformations that can be sampled by proteins. They can be generated by using purely theoretical methods or, as is most often the case, by fitting ensembles of conformations to experimental data that report on the amplitude of protein dynamics. Conformational ensembles have been useful instruments to study fundamental properties of proteins such as the mechanism of molecular recognition, the early stages of protein folding and the mechanism by which structural information propagates through the structures of globular proteins structures via correlated backbone motions. In this chapter I will review the various approaches that have been put forward in the literature to generate conformation ensembles for proteins and present a selection of examples of how such representations of the structural heterogeneity of proteins have been used to explore the fundamental properties of these macromolecules. Finally, I will look ahead at likely future developments in this area, which is important for structural and chemical biology as well as for biophysics.