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

Function in biological systems is exquisitely dependent on spatial and temporal changes in
biomacromolecules. Innumerable biological processes ultimately rely on transduction of …

Over the past 15 years there has been an explosion of research on the dynamical properties
of proteins, largely driven by the emergence of a handful of techniques that are sensitive to …

The physical basis of protein structure, dynamics, and function has been intensely studied
for several decades. Indeed, since the new millennium, there has been a tremendous …

A reversible structural unlocking reaction, in which the close-packed van der Waals
interactions break cooperatively, has been found for the villin headpiece subdomain (HP35) …

The ability to fold proteins on a computer has highlighted the fact that existing force fields
tend to be biased toward a particular type of secondary structure. Consequently, force fields …

NMR relaxation experiments of isotopically labeled proteins provide a wealth of information
on reorientational global and local dynamics on nanosecond and subnanosecond …

Protein dynamics by NMR has been reviewed extensively in recent years [1–10]. These
surveys show decisively that information on structure should be complemented by …

Molecular dynamics simulations are used to analyze the relationship between NMR‐derived
squared generalized order parameters of amide NH groups and backbone entropy. Amide …

Thermodynamic stability is a central requirement for protein function, and one goal of protein
engineering is improvement of stability, particularly for applications in biotechnology. Herein …