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 synergy between structure and dynamics is essential to the function of biological
macromolecules. Thermally driven dynamics on different timescales have been …

The plastic network model (PNM) is used to generate a conformational change pathway for
Escherichia coli adenylate kinase based on two crystal structures, namely that of an open …

Large-scale conformational changes in proteins involve barrier-crossing transitions on the
complex free energy surfaces of high-dimensional space. Such rare events cannot be …

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

NMR relaxation experiments have provided a wealth of information about molecular motions
in macromolecules and ordered fluids. Even though a rigorous theory of spin relaxation is …

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 …

Abstract Domain orientation and dynamics can play an essential role in the function of
multidomain proteins. Lys48‐linked polyubiquitin chains, the principal signal for …

This paper presents an overview of the Fokker-Planck formalism for non-biological magnetic
resonance simulations, describes its existing applications and proposes some novel ones …