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

The last 15 years have seen a paradigm shift in our understanding of protein biochemistry,
with the realization that an unexpectedly high fraction of the human genome codes for …

Misfolding of the protein α-synuclein (aS), which associates with presynaptic vesicles, has
been implicated in the molecular chain of events leading to Parkinson's disease. Here, the …

Protein dynamics are essential for protein function, and yet it has been challenging to
access the underlying atomic motions in solution on nanosecond-to-microsecond time …

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 …

There is growing evidence that structural flexibility plays a central role in the function of
protein molecules. Many of the experimental data come from nuclear magnetic resonance …

1. Introduction.................................................................. 250 2. Magnetic moments,
magnetization, magnetic susceptibility................................ 250 2.1. The Curie …

It is well-established that dynamics are central to protein function; their importance is
implicitly acknowledged in the principles of the Monod, Wyman and Changeux model of …

Orientational restraints such as residual dipolar couplings promise to overcome many of the
problems that traditionally limited liquid-state nuclear magnetic resonance spectroscopy …

NMR spectroscopy is a key method for studying the structure and dynamics of (large)
multidomain proteins and complexes in solution. It plays a unique role in integrated …