Organisms of all domains of life use photoreceptor proteins to sense and respond to light.
The light-sensitivity of photoreceptor proteins arises from bound chromophores such as …

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

▪ Abstract Fourier transform infrared and Raman spectroscopy, solid-state NMR, and X-ray
crystallography have contributed detailed information about the structural changes in the …

The AcrA/AcrB/TolC complex spans the inner and outer membranes of Escherichia coli and
serves as its major drug-resistance pump. Driven by the proton motive force, it mediates the …

The steps in the mechanism of proton transport in bacteriorhodopsin include examples for
most kinds of proton transfer reactions that might occur in a transmembrane pump: proton …

The conduction of protons in the hydrogen-bonded chain of water molecules (or" proton
wire") embedded in the lumen of gramicidin A is studied with molecular dynamics free …

Recent 3-D structures of several intermediates in the photocycle of bacteriorhodopsin (bR)
provide a detailed structural picture of this molecular proton pump in action. In this review …

Rhodopsins are light-sensing proteins used in optogenetics. The word “rhodopsin”
originates from the Greek words “rhodo” and “opsis,” indicating rose and sight, respectively …

The K state, an early intermediate of the bacteriorhodopsin photocycle, contains the excess
free energy used for light-driven proton transport. The energy gain must reside in or near the …

▪ Abstract The recent report of the crystal structure of rhodopsin provides insights concerning
structure-activity relationships in visual pigments and related G protein–coupled receptors …