Results 121 to 130 of about 641,669 (159)

Transducin inhibition of light-dependent rhodopsin phosphorylation: evidence for beta gamma subunit interaction with rhodopsin

, 2014
Rhodopsin kinase was purified from bovine retina rod outer segments as a 62-64-kDa protein that phosphorylated purified rhodopsin reconstituted into egg phosphatidylcholine/phosphatidylethanolamine liposomes.
Johnson, Gary L., Kelleher, Daniel J.
core  

Light-stable rhodopsin. I. A rhodopsin analog reconstituted with a nonisomerizable 11-cis retinal derivative

, 1992
With the aim of preparing a light-stable rhodopsin-like pigment, an analog, II, of 11-cis retinal was synthesized in which isomerization of the C11-C12 cis-double bond is blocked by a cyclohexene ring built around the C10 to C13-methyl.
Khorana, H. G., Knox, B. E., Bhattacharya, S., Ridge, K. D.   +3 more
core  

Korea-Japan Biophysics Collaboration: A journey through microbial rhodopsin research

Biophysics and Physicobiology
Jae-Hyun Park
doaj   +1 more source

Convergent evolution of animal and microbial rhodopsins

Convergent evolution of animal and microbial rhodopsins
Rhodopsins, a family of photoreceptive membrane proteins, contain retinal as a chromophore and were firstly identified as reddish pigments from frog retina in 1876. Since then, rhodopsin-like proteins have been identified mainly from animal eyes. In 1971, a rhodopsin-like pigment was discovered from the archaeon Halobacterium salinarum and named ...
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Microbial Rhodopsins: The Last Two Decades

Annual Review of Microbiology, 2021
Microbial rhodopsins are diverse photoreceptive proteins containing a retinal chromophore and are found in all domains of cellular life and are even encoded in genomes of viruses. These rhodopsins make up two families: type 1 rhodopsins and the recently discovered heliorhodopsins. These families have seven transmembrane helices with similar structures
Oded Béjà, Andrey Rozenberg, Hideki Kandori   +2 more
exaly   +3 more sources

Biochemical Analysis of Microbial Rhodopsins [PDF]

Current Protocols in Microbiology, 2016
AbstractIon‐pumping rhodopsins transfer ions across the microbial cell membrane in a light‐dependent fashion. As the rate of biochemical characterization of microbial rhodopsins begins to catch up to the rate of microbial rhodopsin identification in environmental and genomic sequence data sets, in vitro analysis of their light‐absorbing properties and ...
Jessica Keffer, Julia A Maresca, Kelsey J Miller   +2 more
exaly   +3 more sources

Crystallization of Microbial Rhodopsins

2022
Microbial rhodopsins are light-sensitive transmembrane proteins, evolutionary adapted by various organisms like archaea, bacteria, simple eukaryote, and viruses to utilize solar energy for their survival. A complete understanding of functional mechanisms of these proteins is not possible without the knowledge of their high-resolution structures, which ...
Kirill, Kovalev, Roman, Astashkin, Valentin, Gordeliy, Vadim, Cherezov   +3 more
openaire   +2 more sources

Microbial rhodopsins in the spotlight

Current Opinion in Neurobiology, 2010
The discovery of the light-gated cation channel Channelrhodopsin-2 (ChR2) and the use of the rediscovered light-driven Cl-pump halorhodopsin (HR) as optogenetic tools--genetically encoded switches that enable neurons to be turned on or off with bursts of light--refines the functional study of neurons in larger networks.
Bamann, C., Nagel, G., Bamberg, E.
openaire   +3 more sources

Microbial Rhodopsins

2018
Microbial rhodopsins (MRs) are a large family of photoactive membrane proteins, found in microorganisms belonging to all kingdoms of life, with new members being constantly discovered. Among the MRs are light-driven proton, cation and anion pumps, light-gated cation and anion channels, and various photoreceptors.
Ivan, Gushchin, Valentin, Gordeliy
openaire   +2 more sources

The road to optogenetics: Microbial rhodopsins

Biochemistry (Moscow), 2016
Optogenetics technology (using light-sensitive microbial proteins to control animal cell physiology) is becoming increasingly popular in laboratories around the world. Among these proteins, particularly important are rhodopsins that transport ions across the membrane and are used in optogenetics to regulate membrane potential by light, mostly in ...
E G, Govorunova, L A, Koppel
openaire   +2 more sources