Proteins adopt different higher-order structures (HOS) to enable their unique biological
functions. Understanding the complexities of protein higher-order structures and dynamics …

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

Revised and updated, Chemical Reagents for Protein Modification, Third Edition is an
encyclopedic work describing the many approaches to the site-specific modification of …

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 …

Vibrational spectroscopy provides a direct route to the physicochemical characterization of
molecules. While both IR and Raman spectroscopy have been used for decades to provide …

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

The C≡ C stretching frequencies of terminal alkynes appear in the “clear” window of
vibrational spectra, so they are attractive and increasingly popular as site-specific probes in …

Polarized Raman spectra of the VV component (R∥) and the VH component (R⊥), 2D-COS
synchronous and asynchronous spectra, and HNMR of CH 3 OH/CH 3 CN and CH 3 OH/H 2 …

Determining the pKa of key functional groups is critical to understanding the pH-dependent
behavior of biological proteins and peptide-based biomaterials. Traditionally, 1H NMR …

Conformational transitions displayed by proteins are a classical phenomenon associated
with the structural intricacies that directly influence concomitant functionality. pH-dependent …