Time resolved infrared spectroscopy of biological molecules has provided a wealth of
information relating to structural dynamics, conformational changes, solvation and …

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

Protein dynamics and function is strongly connected to the energy flow taking place.
Myoglobin (Mb) and its mutations are ideal systems to study the process of vibrational …

We construct and analyze disconnectivity graphs to provide the first graphical representation
of the vibrational energy landscape of a protein, in this study β2AR, a G-protein coupled …

Vibrational energy exchange between various degrees of freedom is critical to barrier-
crossing processes in proteins. Hemeproteins are well suited for studying vibrational energy …

The coupling between different vibrational modes in proteins is essential for chemical
dynamics and biological functions and is linked to the propagation of conformational …

Due to advances in methods for site-specific incorporation of unnatural amino acids (UAAs)
into proteins, a large number of UAAs with tailored chemical and/or physical properties have …

Within the protein interior, where we observe various types of interactions, nonuniform flow
of thermal energy occurs along the polypeptide chain and through nonbonded native …

Determining rates of energy transfer across non-covalent contacts for different states of a
protein can provide information about dynamic and associated entropy changes during …

Orthogonal translation is an efficient tool that provides many valuable spectral probes
capable of covering different parts of the electromagnetic spectrum and thus enabling …