Protein Dynamics by Two-dimensional Infrared Spectroscopy

Book excerpt: Proteins function as ensembles of interconverting structures. The motions span from picosecond bond rotations to millisecond and longer subunit displacements. Characterization of functional dynamics on all spatial and temporal scales remains challenging experimentally. Two-dimensional IR spectroscopy (2D IR) is maturing as a powerful approach for investigating proteins and their dynamics. This document outlines the advantages of IR spectroscopy, describes 2D IR and the information it provides, and introduces vibrational groups for protein analysis. Following this introduction, example studies are presented that illustrate the power and versatility of 2D IR for characterizing protein dynamics. The thesis concludes with a brief discussion of the outlook for biomolecular 2D IR.