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 …

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 …

Protein dynamics and interactions in myoglobin (Mb) were characterized via two vibrational
dynamics labels (VDLs): a genetically incorporated site-specific azide (Az) bearing …

A series of two-dimensional infrared vibrational echo experiments performed on nitrile-
labeled villin headpiece [HP35-(CN) 2] is described. HP35 is a small peptide composed of …

There has been great interest in the development of stable, inexpensive, efficient catalysts
capable of reducing aqueous protons to hydrogen (H2), an alternative to fossil fuels. While …

Proteins are complex, heterogeneous macromolecules that exist as ensembles of
interconverting states on a complex energy landscape. A complete, molecular-level …

Cytochrome (cyt) P450s hydroxylate a variety of substrates that can differ widely in their
chemical structure. The importance of these enzymes in drug metabolism and other …

Understanding the role of coherent electronic motion is expected to resolve general
questions of importance in macromolecular energy transfer. We demonstrate a novel …

This review examines low-frequency vibrational modes of proteins and their coupling to
enzyme catalytic sites. That protein motions are critical to enzyme function is clear, but the …

Myoglobin (Mb) double mutant T67R/S92D displays peroxidase enzymatic activity in
contrast to the wild type protein. The CO adduct of T67R/S92D shows two CO absorption …