Infrared (IR) spectroscopy is a highly sensitive technique that provides complete information
on chemical compositions. The IR spectra of proteins or peptides give rise to nine …

Supramolecular gels are a fascinating class of soft materials. Their gelators can self-
assemble into nano-or micro-scale superstructures, such as fibers, ribbons, sheets and …

Protein stability is a topic of major interest for the biotechnology, pharmaceutical and food
industries, in addition to being a daily consideration for academic researchers studying …

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 …

Two-dimensional (2D) optical spectroscopy utilizing multiple ultrafast coherent laser pulses
in the infrared or UV-vis frequency range has been used to study protein structure and …

Two-Dimensional Optical Spectroscopy discusses the principles and applications of newly
emerging two-dimensional vibrational and optical spectroscopy techniques. It provides a …

We review two-dimensional infrared (2D IR) spectroscopy of the amide I protein backbone
vibration. Amide I modes are known for secondary structural sensitivity derived from their …

A theoretical description of femtosecond two-dimensional electronic spectroscopy of
multichromophoric systems is presented. Applying the stationary phase approximation to the …

Applications of 2D IR Spectroscopy to Peptides, Proteins, and Hydrogen-Bond Dynamics | The
Journal of Physical Chemistry B ACS ACS Publications C&EN CAS Find my institution Log In …

The capability of 2D IR spectroscopy to elucidate time-evolving structures is enhanced by a
programmable mid-IR pulse shaper that greatly improves the ease, speed, and accuracy of …