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 …

In this article, approaches towards the paramagnetic tagging of diamagnetic proteins are
reviewed. Alignment can be achieved by adding paramagnetic fusion proteins or peptides to …

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 …

Cryptic pockets expand the scope of drug discovery by enabling targeting of proteins
currently considered undruggable because they lack pockets in their ground state structures …

A molecular-level understanding of the function of a protein requires knowledge of both its
structural and dynamic properties. NMR spectroscopy allows the measurement of …

Characterization of protein dynamics by solid-state NMR spectroscopy requires robust and
accurate measurement protocols, which are not yet fully developed. In this study, we …

Correlated motions in proteins can mediate fundamental biochemical processes such as
signal transduction and allostery. The mechanisms that underlie these processes remain …

Residual dipolar couplings (RDCs) provide information about the dynamic average
orientation of inter-nuclear vectors and amplitudes of motion up to milliseconds. They …

It is proposed to convert nuclear Overhauser effects (NOEs) into relatively precise distances
for detailed structural studies of proteins. To this purpose, it is demonstrated that the …

This review describes two rotating-frame (R 1 ρ) relaxation dispersion methods, namely the
Bloch-McConnell Relaxation Dispersion and the Near-rotary Resonance Relaxation …