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 …

Two-dimensional infrared (2D IR) spectroscopy has recently emerged as a powerful tool
with applications in many areas of scientific research. The inherent high time resolution …

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 …

The high concentration of macromolecules in the crowded cellular interior influences
different thermodynamic and kinetic properties of proteins, including their structural …

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 …

Protein–protein complex assembly is one of the major drivers of biological response.
Understanding the mechanisms of protein oligomerization/dimerization would allow one to …

The center line slope (CLS) method is often used to extract the frequency-frequency
correlation function (FFCF) from 2D IR spectra to delineate dynamics and to identify …

Here, we present a new analysis program, AIM, that allows extracting the vibrational amide-I
Hamiltonian using molecular dynamics trajectories for protein infrared spectroscopy …

Biological functions frequently require protein–protein interactions that involve secondary
and tertiary structural perturbation. Here we study protein–protein dissociation and …

The protein hormone insulin exists in various oligomeric forms, and a key step in binding its
cellular receptor is dissociation of the dimer. This dissociation process and its corresponding …