The perspective reviews quantitative investigations of chemical exchange phenomena in
proteins and other biological macromolecules using NMR spectroscopy, particularly …

Functioning proteins do not remain fixed in a unique structure, but instead they sample a
range of conformations facilitated by motions within the protein. Even in the native state, a …

Knowing the 3D structures formed by the various conformations populating the RNA free-
energy landscape, their relative abundance, and kinetic interconversion rates is required to …

Human ubiquitin has been extensively characterized using a variety of experimental and
computational methods and has become an important model for studying protein dynamics …

Accurate mechanistic description of structural changes in biomolecules is an increasingly
important topic in structural and chemical biology. Markov models have emerged as a …

In the present work, we provide a dielectric study on two differently concentrated aqueous
lysozyme solutions in the frequency range from 1MHz to 40GHz and for temperatures from …

Intrinsically disordered proteins and intrinsically disordered regions (IDRs) are ubiquitous in
the eukaryotic proteome. The description and understanding of their conformational …

Understanding the molecular determinants underlying protein function requires the
characterization of both structure and dynamics at atomic resolution. Nuclear relaxation …

Many biological processes depend on allosteric communication between different parts of a
protein, but the role of internal protein motion in propagating signals through the structure …

It has recently been proposed by Gunasakaran et al. that allostery may be an intrinsic
property of all proteins. Here, we develop a computational method that can determine and …