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

Infrared difference spectroscopy probes vibrational changes of proteins upon their
perturbation. Compared with other spectroscopic methods, it stands out by its sensitivity to …

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 …

Quantum mechanics provides the most accurate microscopic description of the world around
us, yet the interface between quantum mechanics and biology is only now being explored …

Numerous linear and non-linear spectroscopic techniques have been developed to
elucidate structural and functional information of complex systems ranging from natural …

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 …

Amyloid formation has been implicated in the pathology of over 20 human diseases, but the
rational design of amyloid inhibitors is hampered by a lack of structural information about …

The M2 protein of influenza A viruses forms a tetrameric pH-activated proton-selective
channel that is targeted by the amantadine class of antiviral drugs. Its ion channel function …

Infrared (IR) spectroscopy of the amide I band has been widely utilized for the analysis of
peptides and proteins. Theoretical modeling of IR spectra of proteins requires an accurate …

Two-dimensional infrared spectroscopy of amide I vibrations is increasingly being used to
study the structure and dynamics of proteins and peptides. Amide I, a primarily carbonyl …