Function in biological systems is exquisitely dependent on spatial and temporal changes in
biomacromolecules. Innumerable biological processes ultimately rely on transduction of …

Enzyme catalysis is an inherently dynamic process. Binding and release of ligands is often
accompanied by conformational changes, both subtle and dramatic (reviewed more …

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 …

Over the past 15 years there has been an explosion of research on the dynamical properties
of proteins, largely driven by the emergence of a handful of techniques that are sensitive to …

Large-scale conformational changes in proteins are often associated with the binding of a
substrate. Because conformational changes may be related to the function of an enzyme …

Elucidating the complex interplay between protein structure and dynamics is a prerequisite
to an understanding of both function and adaptation in proteins. Unfortunately, it has been …

Enzyme function is often dependent on fluctuations between inactive and active structural
ensembles. Adenylate kinase isolated from Escherichia coli (AKe) is a small …

Proteins can bind target molecules through either induced fit or conformational selection
pathways. In the conformational selection model, a protein samples a scarcely populated …

The two-body Slowly Relaxing Local Structure (SRLS) model was applied to 15N NMR spin
relaxation in proteins and compared with the commonly used original and extended model …

During its late steps, the mitochondrial iron–sulfur cluster (ISC) assembly machinery leads to
the formation of [4Fe‐4S] clusters. In vivo studies revealed that several proteins are …