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

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 …

Applications of 2D IR Spectroscopy to Peptides, Proteins, and Hydrogen-Bond Dynamics | The
Journal of Physical Chemistry B Recently Viewedclose modal ACS ACS Publications C&EN …

Infrared spectroscopy has played an instrumental role in the study of a wide variety of
biological questions. However, in many cases, it is impossible or difficult to rely on the …

Elucidating the underlying molecular mechanisms of protein folding and function is a very
exciting and active research area, but poses significant challenges. This is due in part to the …

This paper presents an overview of recent experiments and theoretical developments aimed
at using vibrational spectroscopy to understand the structure and dynamics of nitrile-labeled …

Infrared (IR) band shifts of isolated vibrational transitions can serve as quantitative and
directional probes of local electrostatic fields, due to the vibrational Stark effect. However …

Electrostatic interactions provide a primary connection between a protein's three-
dimensional structure and its function. Infrared probes are useful because vibrational …

Noncovalent interactions, in particular the hydrogen bonds and nonspecific long-range
electrostatic interactions are fundamental to biomolecular functions. A molecular …

Amyloid diseases, including neurodegenerative diseases such as Alzheimer's and
Parkinson's, are linked to a poorly understood progression of protein misfolding and …