Infrared difference spectroscopy probes vibrational changes of proteins upon their
perturbation. Compared with other spectroscopic methods, it stands out by its sensitivity to …

Conspectus Light activated proteins are at the heart of photobiology and optogenetics, so
there is wide interest in understanding the mechanisms coupling optical excitation to protein …

The orange carotenoid protein (OCP) is a two-domain photoactive protein that noncovalently
binds an echinenone (ECN) carotenoid and mediates photoprotection in cyanobacteria. In …

Blue light sensing using flavin (BLUF) domains constitute a family of flavin-binding
photoreceptors of bacteria and eukaryotic algae. BLUF photoactivation proceeds via a light …

We describe the development, implementation, and application of a polarizable QM/MM
strategy, based on the AMOEBA polarizable force field, for calculating molecular properties …

The hydrogen bonding network that surrounds the flavin in blue light using flavin adenine
dinucleotide (BLUF) photoreceptors plays a crucial role in sensing and communicating the …

We present a dual-amplifier laser system for time-resolved multiple-probe infrared (IR)
spectroscopy based on the ytterbium potassium gadolinium tungstate (Yb: KGW) laser …

Dynamical changes in protein structures are essential for protein function and occur over
femtoseconds to seconds timescales. X‐ray free electron lasers have facilitated …

Blue light sensor using flavin (BLUF) proteins consist of flavin-binding BLUF domains and
functional domains. Upon blue light excitation, the hydrogen bond network around the flavin …

Photoreceptor proteins have been used to study how protein conformational changes are
induced by alterations in their environments and how their signals are transmitted to …