BACKGROUND Biomolecular mechanisms are typically inferred from static structural
“snapshots” obtained by x-ray crystallography, nuclear magnetic resonance (NMR) …

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

Nuclear magnetic resonance (NMR) is widely used across many fields of science because
of the rich data it produces, and some of the most valuable data come from studies of …

Hydrogels and organogels are semi-solid systems, in which a liquid phase is immobilized by
a three-dimensional network composed of self-assembled, intertwined polymer/gelator …

Long-range distance measurements based on paramagnetic relaxation enhancement (PRE)
in NMR, quantification of surface water dynamics near biomacromolecules by Overhauser …

The nuclear Overhauser enhancement or effect (NOE) is the most important measure in
liquid-state NMR with macromolecules. Thus, the NOE is the subject of numerous reviews …

Molecular motion of biopolymers in vivo is known to be strongly influenced by the high
concentration of organic matter inside cells, usually referred to as crowding conditions. To …

It is now well accepted that structures alone cannot explain protein function and biochemical
data. Indeed, dynamics on different timescales play an important role in their function. Many …

This article reviews the application of solid-state 2 H nuclear magnetic resonance (NMR)
spectroscopy for investigating the deformation of lipid bilayers at the atomistic level. For …

The Liouville space spin relaxation theory equations are reformulated in such a way as to
avoid the computationally expensive Hamiltonian diagonalization step, replacing it by …