Biomolecular hydration dynamics probed with 2D-IR spectroscopy: From dilute solution to a macromolecular crowd

Although it is well known that water is essential for biological function, it has been a challenge to determine how water behaves near biomacromolecular interfaces, and what role water plays in influencing the dynamics of the biochemical machinery. By adopting a vibrational labeling strategy coupled with ultrafast two-dimensional infrared (2D-IR) spectroscopy, it has recently become possible to study hydration dynamics, site specifically at the surface of proteins and model membranes. We review our recent progress in measuring hydration dynamics in contexts ranging from small-molecule solutes to biomacromolecules in dilute, viscous, and crowded environments.

Graphical abstractThe combination of site-specific chemical labeling, ultrafast two-dimensional infrared spectroscopy and molecular dynamics simulation has enabled detailed investigations of biomolecule hydration dynamics.Figure optionsDownload full-size imageDownload as PowerPoint slide