The light sensor of vertebrate scotopic (low-light) vision, rhodopsin, is a G-protein-coupled
receptor comprising a polypeptide chain with bound chromophore, 11-cis-retinal, that …

Allosteric signaling in biological molecules, which may be viewed as specific action at a
distance due to localized perturbation upon binding of ligands or changes in environmental …

Investigations of lipid membranes using NMR spectroscopy generally require isotopic
labeling, often precluding structural studies of complex lipid systems. Solid-state 13 C magic …

Opsin, the rhodopsin apoprotein, was recently shown to be an ATP-independent flippase (or
scramblase) that equilibrates phospholipids across photoreceptor disc membranes in …

Many transmembrane receptors have a desensitized state, in which they are unable to
respond to external stimuli. The family of microbial rhodopsin proteins includes one such …

Variable-temperature electrospray ionization (vT-ESI) native mass spectrometry (nMS) is
used to determine the thermodynamics for stepwise binding of up to 14 ATP molecules to …

Rhodopsin is the light receptor in rod photoreceptor cells of the retina that initiates scotopic
vision. In the dark, rhodopsin is bound to the chromophore 11-cis retinal, which locks the …

G protein-coupled receptors (GPCRs) are central to many fundamental cellular signaling
pathways. They transduce signals from the outside to the inside of cells in physiological …

Rhodopsin, a prototypical G protein-coupled receptor, is a membrane protein that can sense
dim light. This highly effective photoreceptor is known to be sensitive to the composition of its …

This article reviews the application of solid-state 2 H nuclear magnetic resonance (NMR)
spectroscopy for investigating the deformation of lipid bilayers at the atomistic level. For …