Carbon monoxide (CO) has been firmly established as an endogenous signaling molecule
with a variety of pathophysiological and pharmacological functions, including …

Time-resolved small-and wide-angle X-ray scattering studies of proteins in solution based
on the pump-probe approach unveil structural information from intermediates over a broad …

Correlated motions of proteins are critical to function, but these features are difficult to
resolve using traditional structure determination techniques. Time-resolved X-ray methods …

Relevant events during protein function such as ligand binding/release and interaction with
substrates or with light are often accompanied by out-of-equilibrium structural dynamics …

ABSTRACT A major goal in biomedical science is to move beyond static images of proteins
and other biological macromolecules to the internal dynamics underlying their function. This …

Background Human hemoglobin is an allosteric protein that exerts exquisite control over
ligand binding through large-scale conformational changes. The two-state model without …

The protein folding process often proceeds through partially folded transient states.
Therefore, a structural understanding of these disordered states is crucial for developing …

The structure of a protein is closely related to its biological function. In this regard, structural
changes, as well as static structures, have been scrutinized as essential elements in …

Understanding and controlling protein motion at atomic resolution is a hallmark challenge
for structural biologists and protein engineers because conformational dynamics are …

In the past few decades, prediction of macromolecular structures beyond the native
conformation has been aided by the development of molecular dynamics (MD) protocols …