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

How do proteins fold, and why do they fold in that way? This Perspective integrates earlier
and more recent advances over the 50-y history of the protein folding problem, emphasizing …

Proteins are inherently flexible at ambient temperature. At equilibrium, they are
characterized by a set of conformations that undergo continuous exchange within a …

In-cell NMR is an isotope-aided multi-dimensional NMR technique that enables
observations of conformations and functions of proteins in living cells at the atomic level …

Recent work has largely completed our understanding of the hydrogen-exchange chemistry
of unstructured proteins and nucleic acids. Some of the high-energy structural fluctuations …

This discussion, prepared for the Protein Society's symposium honoring the 100th
anniversary of Kaj Linderstrøm‐Lang, shows how hydrogen exchange approaches initially …

▪ Abstract Mass spectrometry has provided a powerful method for monitoring hydrogen
exchange of protein backbone amides with deuterium from solvent. In comparison to …

▪ Abstract In order to solve the immensely difficult protein-folding problem, it will be
necessary to characterize the barriers that slow folding and the intermediate structures that …

To examine the relationship between protein structural dynamics and measurable hydrogen
exchange (HX) data, the detailed exchange behavior of most of the backbone amide …

Abstract I. Introduction 38 A. Protein Conformations and Dynamics 38 B. Protein‐Energy
Landscapes: The Folding Problem and Dynamics in the Native State 38 1. Protein …