Molecular recognition is central to all biological processes. For the past 50 years,
Koshland's' induced fit'hypothesis has been the textbook explanation for molecular …

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

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 …

Noncovalent binding interactions between proteins are the central physicochemical
phenomenon underlying biological signaling and functional control on the molecular level …

Protein-protein recognition and binding are governed by diffusion, noncovalent forces and
conformational flexibility, entangled in a way that only molecular dynamics simulations can …

Protein folding and molecular recognition and binding provide the basis for life on earth. The
native 3D structure of a protein is necessary for its biological function; and the …

Protein function can be modulated or dictated by the amplitude and timescale of
biomolecular motion, therefore it is imperative to study protein dynamics. Nuclear Magnetic …

Abstract Here we present Cys-Ph-TAHA, a new nonadentate lanthanide tag for the
paramagnetic labelling of proteins. The tag can be easily synthesized and is …

The relaxation of long‐lived states (LLS) corresponds to the slow return to statistical thermal
equilibrium between symmetric and antisymmetric proton spin states. This process is …

NMR spectroscopy is the leading technique to characterize protein internal dynamics at the
atomic level and on multiple time scales. However, the structural interpretation of the …