Biophysical characterization of microbial rhodopsins with DSE motif [PDF]
Biophysics and Physicobiology, 2023 Microbial rhodopsins are photoreceptive transmembrane proteins that transport ions or regulate other intracellular biological processes. Recent genomic and metagenomic analyses found many microbial rhodopsins with unique sequences distinct from known ...
María del Carmen Marín +5 more
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Graphs of protein-water hydrogen bond networks to dissect structural movies of ion-transfer microbial rhodopsins [PDF]
Frontiers in Chemistry, 2023 Microbial rhodopsins are membrane proteins that use the energy absorbed by the covalently bound retinal chromophore to initiate reaction cycles resulting in ion transport or signal transduction.
Éva Bertalan +2 more
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Understanding Colour Tuning Rules and Predicting Absorption Wavelengths of Microbial Rhodopsins by Data-Driven Machine-Learning Approach [PDF]
Scientific Reports, 2018 The light-dependent ion-transport function of microbial rhodopsin has been widely used in optogenetics for optical control of neural activity. In order to increase the variety of rhodopsin proteins having a wide range of absorption wavelengths, the light
Masayuki Karasuyama +4 more
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Imaging Voltage with Microbial Rhodopsins [PDF]
Frontiers in Molecular Biosciences, 2021 Membrane potential is the critical parameter that reflects the excitability of a neuron, and it is usually measured by electrophysiological recordings with electrodes.
Xiao Min Zhang +3 more
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Monitoring the Progression of Cell-Free Expression of Microbial Rhodopsins by Surface Enhanced IR Spectroscopy: Resolving a Branch Point for Successful/Unsuccessful Folding [PDF]
Frontiers in Molecular Biosciences, 2022 The translocon-unassisted folding process of transmembrane domains of the microbial rhodopsins sensory rhodopsin I (HsSRI) and II (HsSRII), channelrhodopsin II (CrChR2), and bacteriorhodopsin (HsBR) during cell-free expression has been investigated by ...
Kenichi Ataka +5 more
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Solid-state NMR of the retinal protonated Schiff base in microbial rhodopsins [PDF]
Magnetic Resonance LettersRhodopsin is a seven-helical transmembrane protein with a retinal chromophore covalently bound to a conserved lysine in helix G via a retinal protonated Schiff base (RPSB). Microbial rhodopsins absorb light through chromophore and play a fundamental role
Sari Kumagai, Izuru Kawamura
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QuasAr Odyssey: the origin of fluorescence and its voltage sensitivity in microbial rhodopsins [PDF]
Nature Communications, 2022 The authors present an in-depth investigation of excited state dynamics and molecular mechanism of the voltage sensing in microbial rhodopsins. Using a combination of spectroscopic investigations and molecular dynamics simulations, the study proposes the
Arita Silapetere +16 more
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Ion-Pumping Microbial Rhodopsins [PDF]
Frontiers in Molecular Biosciences, 2015 Rhodopsins are light-sensing proteins used in optogenetics. The word rhodopsin originates from the Greek words rhodo and opsis, indicating rose and sight, respectively. Although the classical meaning of rhodopsin is the red-colored pigment in our eyes,
Hideki eKandori
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Expression of microbial rhodopsins in Escherichia coli and their extraction and purification using styrene-maleic acid copolymers [PDF]
STAR Protocols, 2022 Summary: Microbial rhodopsins are photoreceptive membrane proteins showing various light-dependent biological activities. Styrene-maleic acid (SMA) copolymers spontaneously form nanoscale lipid particles containing membrane proteins and associated lipids
Keiichi Kojima, Yuki Sudo
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Microbial Rhodopsins: Structural–Functional Mechanisms and the Design of Optogenetic Silencing Tools—With Emphasis on Halorubrum Archaeorhodopsins [PDF]
BiologyMicrobial rhodopsins are light-sensitive membrane proteins that use retinal as a covalent chromophore and adopt a seven-transmembrane α-helical fold. They are widely distributed across archaea, bacteria, algae, and fungi and mediate diverse functions ...
Luomeng Chao, Yuxia Yang
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