The growing interest for comparing protein internal dynamics owes much to the realisation
that protein function can be accompanied or assisted by structural fluctuations and …

With the recent advances in ultrabright electron and x-ray sources, it is now possible to
extend crystallography to the femtosecond time domain to literally light up atomic motions …

Advances in sequencing techniques and statistical methods have made it possible not only
to predict sequences of ancestral proteins but also to identify thousands of mutations in the …

Abstract The interface of protein structural biology, protein biophysics, molecular evolution,
and molecular population genetics forms the foundations for a mechanistic understanding of …

β-lactamases are produced by many modern bacteria as a mechanism of resistance toward
β-lactam antibiotics, the most common antibiotics in use. β-lactamases, however, are ancient …

This review documents the development of high–bunch charge electron pulses with
sufficient combined spatiotemporal resolution and intensity to literally light up atomic …

Motivation: The function of a protein depends not only on its structure but also on its
dynamics. This is at the basis of a large body of experimental and theoretical work on protein …

Proteins are intrinsically flexible molecules. The role of internal motions in a protein's
designated function is widely debated. The role of protein structure in enzyme catalysis is …

Proteins are dynamical entities that undergo a plethora of conformational changes,
accomplishing their biological functions. Molecular dynamics simulation and normal mode …

Protein structure is dynamic: the intrinsic flexibility of polypeptides facilitates a range of
conformational fluctuations, and individual protein chains can assemble into complexes …