Proteins exhibit structural fluctuations over decades of time scales. From the picosecond
side chain motions to aggregates that form over the course of minutes, characterizing protein …

Controlling the activity of proteins with azobenzene photoswitches is a potent tool for
manipulating their biological function. With the help of light, it is possible to change binding …

Transition-metal complexes, which exhibit photobasic properties, are highly promising for
chemical applications where the proton abstraction represents one key step. Photobases …

Disordered proteins often undergo a stimuli-responsive, disorder-to-order transition which
facilitates dynamic processes that modulate the physiological activities and material …

Protein folding research stalled for decades because conventional experiments indicated
that proteins fold slowly and in single strokes, whereas theory predicted a complex interplay …

The advent of the X-ray free electron laser (XFEL) in the last decade created the discipline of
serial crystallography but also the challenge of how crystal samples are delivered to X-ray …

ortho-Nitrobenzaldehyde (o NBA) is a well-known photoactivated acid and a prototypical
photolabile nitro-aromatic compound. Despite extensive investigations, the ultrafast …

Controlled initiation of biochemical events and in particular of protein activity is a powerful
tool in biochemical research. Specifically, optical trigger signals are an attractive approach …

While the theory of protein folding is well developed, including concepts such as rugged
energy landscape, folding funnel, etc., the same degree of understanding has not been …

Control of proton transfer is relevant to many areas in chemistry, particularly in catalysis
where the kinetics of (de) protonation reactions are often rate limiting. Photobases, which …