Paramagnetic chemical probes have been used in electron paramagnetic resonance (EPR)
and nuclear magnetic resonance (NMR) spectroscopy for more than four decades. Recent …

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

Protein structure and dynamics can be characterized on the atomistic level with both nuclear
magnetic resonance (NMR) experiments and molecular dynamics (MD) simulations. Here …

Motions play a vital role in the functions of many proteins. Discrete conformational transitions
to excited states, happening on timescales of hundreds of microseconds, have been …

Solution-state NMR relaxation experiments are the cornerstone to study internal protein
dynamics at an atomic resolution on time scales that are faster than the overall rotational …

Motions of proteins are essential for the performance of their functions. Aliphatic protein side
chains and their motions play critical roles in protein interactions: for recognition and binding …

Amino-acid side-chain properties in proteins are key determinants of protein function. NMR
spin relaxation of side chains is an important source of information about local protein …

Protein methyl groups have recently been the subject of much attention in NMR
spectroscopy because of the opportunities that they provide to obtain information about the …

Allosteric regulation is a key component of cellular communication, but the way in which
information is passed from one site to another within a folded protein is not often clear. While …

Overwhelming evidence now illustrates the defining role of atomic-scale protein flexibility in
biological events such as allostery, cell signaling, and enzyme catalysis. Over the years …