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 …

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

Molecular vibrational polaritons, a hybridized quasiparticle formed by the strong coupling
between molecular vibrational modes and photon cavity modes, have attracted tremendous …

Nuclear–electronic (vibronic) coupling is increasingly recognized as a mechanism of major
importance in controlling the light-induced function of molecular systems. It was recently …

The coupling between electrons and protons and the long-range transport of protons play
important roles throughout biology. Biomimetic systems derived from benzimidazole-phenol …

Coupling infrared (IR) spectroscopy to microfluidic devices provides a powerful tool for
characterizing complex chemical and biochemical reactions. Examples of microfluidic …

Abstract Two-dimensional infrared (2D-IR) spectroscopy is a powerful technique capable of
accessing structure and dynamics with ultrafast time resolution in a wide range of chemical …

Fluorescence-encoded infrared (FEIR) spectroscopy is an ultrafast technique that uses a
visible pulse to up-convert information about IR-driven vibrations into a fluorescent …

Bimolecular reactions in the gas phase exhibit rich and varied dynamical behaviour, but
whether a profound knowledge of the mechanisms of isolated reactive collisions can …

Over the last decade, ultrafast two-dimensional infrared (2D IR) spectroscopy has been
greatly advanced in a variety of aspects and is becoming a more exciting vibrational tool for …