Vibrational spectroscopy is an essential tool in chemical analyses, biological assays, and
studies of functional materials. Over the past decade, various coherent nonlinear vibrational …

The structure and function of biomolecules are strongly influenced by their hydration shells.
Structural fluctuations and molecular excitations of hydrating water molecules cover a broad …

Proteins exhibit structural fluctuations over decades of time scales. From the picosecond
side chain motions to aggregates that form over the course of minutes, characterizing protein …

Protein hydration shell dynamics play an important role in biochemical processes including
protein folding, enzyme function, and molecular recognition. We present here a comparison …

Infrared spectroscopy has played an instrumental role in the study of a wide variety of
biological questions. However, in many cases, it is impossible or difficult to rely on the …

Structural modifications to interacting systems frequently lead to changes in both the
enthalpy (heat) and entropy of the process that compensate each other, so that the Gibbs …

Vibrational spectroscopy provides a direct route to the physicochemical characterization of
molecules. While both IR and Raman spectroscopy have been used for decades to provide …

Historically it has been virtually impossible to experimentally determine the contribution of
residual protein entropy to fundamental protein activities such as the binding of ligands …

There is considerable evidence for the slaving of biomolecular dynamics to the motions of
the surrounding solvent environment, but to date there have been few direct experimental …

The advent of laser-based sources of ultrafast infrared pulses has extended the study of very
fast molecular dynamics to the observation of processes manifested through their effects on …