Search results for "Opsins"

showing 10 items of 26 documents

Food Sensation Modulates Locomotion by Dopamine and Neuropeptide Signaling in a Distributed Neuronal Network

2018

Finding food and remaining at a food source are crucial survival strategies. We show how neural circuits and signaling molecules regulate these food-related behaviors in Caenorhabditis elegans. In the absence of food, AVK interneurons release FLP-1 neuropeptides that inhibit motorneurons to regulate body posture and velocity, thereby promoting dispersal. Conversely, AVK photoinhibition promoted dwelling behavior. We identified FLP-1 receptors required for these effects in distinct motoneurons. The DVA interneuron antagonizes signaling from AVK by releasing cholecystokinin-like neuropeptides that potentiate cholinergic neurons, in response to dopaminergic neurons that sense food. Dopamine al…

0301 basic medicineCell signalingSensory Receptor CellsInterneuronDopamineSensationNeuropeptideOptogeneticsBiologyReceptors DopamineAnimals Genetically Modified03 medical and health sciencesChannelrhodopsinsDopamineNeural PathwaysBiological neural networkmedicineAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsGeneral NeuroscienceNeuropeptidesdigestive oral and skin physiologyDopaminergicOptogenetics030104 developmental biologymedicine.anatomical_structureFoodDopamine receptorCalciumNeuroscienceLocomotionmedicine.drugNeuron
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Convergence of Cortical and Sensory Driver Inputs on Single Thalamocortical Cells

2013

Ascending and descending information is relayed through the thalamus via strong, "driver" pathways. According to our current knowledge, different driver pathways are organized in parallel streams and do not interact at the thalamic level. Using an electron microscopic approach combined with optogenetics and in vivo physiology, we examined whether driver inputs arising from different sources can interact at single thalamocortical cells in the rodent somatosensory thalamus (nucleus posterior, POm). Both the anatomical and the physiological data demonstrated that ascending driver inputs from the brainstem and descending driver inputs from cortical layer 5 pyramidal neurons converge and interac…

MalePatch-Clamp TechniquesCognitive NeuroscienceThalamusBiotinMice TransgenicSensory systemOptogeneticsBiologySomatosensory systemFunctional LateralityMembrane PotentialsMiceCellular and Molecular NeuroscienceChannelrhodopsinsMicroscopy Electron TransmissionThalamusNeural PathwaysmedicineAnimalsPhytohemagglutininsRats WistarCerebral CortexNeuronsExcitatory Postsynaptic PotentialsDextransddc:Ratsmedicine.anatomical_structureCerebral cortexSynapsesRecurrent thalamo-cortical resonanceVesicular Glutamate Transport Protein 2BrainstemNucleusNeuroscienceCerebral Cortex
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Interfacial water structure controls protein conformation.

2007

A phenomenological theory of salt-induced Hofmeister phenomena is presented, based on a relation between protein solubility in salt solutions and protein-water interfacial tension. As a generalization of previous treatments, it implies that both kosmotropic salting out and chaotropic salting in are manifested via salt-induced changes of the hydrophobic/hydrophilic properties of protein-water interfaces. The theory is applied to describe the salt-dependent free energy profiles of proteins as a function of their water-exposed surface area. On this basis, three classes of protein conformations have been distinguished, and their existence experimentally demonstrated using the examples of bacter…

DYNAMICSMECHANISMKosmotropicProtein ConformationSURFACE-TENSIONSurface tensionchemistry.chemical_compoundProtein structureMaterials ChemistryPhysical and Theoretical ChemistryPURPLE MEMBRANESPECTROSCOPYbiologySTABILITYBACTERIORHODOPSINMyoglobinSALTTemperatureWaterBacteriorhodopsinSTABILITY MECHANISMSurfaces Coatings and FilmsION SPECIFICITYChaotropic agentCrystallographyMyoglobinchemistryTEMPERATURE-DEPENDENCEChemical physicsStructural stabilityBacteriorhodopsinsbiology.proteinSalting outThermodynamicsThe journal of physical chemistry. B
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Coreconstitution of bacterial ATP synthase with monomeric bacteriorhodopsin into liposomes. A comparison between the efficiency of monomeric bacterio…

1987

The conditions for coreconstitution of a bacterial ATP synthase and bacteriorhodopsin into lecithin liposomes and for light driven ATP synthesis have been optimized. A rate of maximally 280 nmol ATP min-1 mg ATP synthase-1 was achieved with monomerized bacteriorhodopsin compared with a rate of up to 45 nmol ATP min-1 mg-1 found for proteoliposomes containing bacteriorhodopsin in the form of purple membrane patches. The different rates are explained by the finding that monomeric bacteriorhodopsin is more homogeneously distributed among the liposomes than the purple membrane patches. The final activities depended on both the purification method for the two proteins and the coreconstitution pr…

Liposomefood.ingredientLightATP synthasebiologyChemiosmosisKineticsBacteriorhodopsinRhodospirillum rubrumBiochemistryLecithinKineticsProton-Translocating ATPaseschemistry.chemical_compoundMonomerfoodMembranechemistryBiochemistryBacteriorhodopsinsLiposomesbiology.proteinEuropean Journal of Biochemistry
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Changes in the hydrogen-bonding strength of internal water molecules and cysteine residues in the conductive state of channelrhodopsin-1

2014

Water plays an essential role in the structure and function of proteins, particularly in the less understood class of membrane proteins. As the first of its kind, channelrhodopsin is a light-gated cation channel and paved the way for the new and vibrant field of optogenetics, where nerve cells are activated by light. Still, the molecular mechanism of channelrhodopsin is not understood. Here, we applied time-resolved FT-IR difference spectroscopy to channelrhodopsin-1 from Chlamydomonas augustae. It is shown that the (conductive) P2(380) intermediate decays with τ ≈ 40 ms and 200 ms after pulsed excitation. The vibrational changes between the closed and the conductive states were analyzed in…

Models Molecular570StereochemistryGeneral Physics and AstronomyInfrared spectroscopy530Ion Channelschemistry.chemical_compoundAmideRhodopsins MicrobialSpectroscopy Fourier Transform InfraredSide chainMoleculePeptide bondCysteinePhysical and Theoretical ChemistryPlant Proteinschemistry.chemical_classificationHydrogen bondChlamydomonasWaterFísicaHydrogen BondingQuímicaCrystallographychemistryThiolProteïnesCysteineThe Journal of Chemical Physics
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pH-sensitive vibrational probe reveals a cytoplasmic protonated cluster in bacteriorhodopsin

2017

Infrared spectroscopy has been used in the past to probe the dynamics of internal proton transfer reactions taking place during the functional mechanism of proteins but has remained mostly silent to protonation changes in the aqueous medium. Here, by selectively monitoring vibrational changes of buffer molecules with a temporal resolution of 6 µs, we have traced proton release and uptake events in the light-driven proton-pump bacteriorhodopsin and correlate these to other molecular processes within the protein. We demonstrate that two distinct chemical entities contribute to the temporal evolution and spectral shape of the continuum band, an unusually broad band extending from 2,300 to well…

0301 basic medicineModels MolecularCytoplasmNuclear TheoryMolecular ConformationInfrared spectroscopyIonic bondingProtonationBuffers010402 general chemistry53001 natural sciences03 medical and health sciencesDeprotonationSpectroscopy Fourier Transform InfraredMoleculeNuclear ExperimentMultidisciplinarybiologyChemistryWaterBacteriorhodopsinHydrogen-Ion Concentration0104 chemical sciencesKinetics030104 developmental biologyPNAS PlusChemical physicsCytoplasmTemporal resolutionBacteriorhodopsinsbiology.proteinPhysics::Accelerator PhysicsProtonsMetabolic Networks and PathwaysProtein Binding
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Potential Second-Harmonic Ghost Bands in Fourier Transform Infrared (FT-IR) Difference Spectroscopy of Proteins

2018

Fourier transform infrared (FT-IR) difference absorption spectroscopy is a common method for studying the structural and dynamical aspects behind protein function. In particular, the 2800–1800 cm−1 spectral range has been used to obtain information about internal (deuterated) water molecules, as well as site-specific details about cysteine residues and chemically modified and artificial amino acids. Here, we report on the presence of ghost bands in cryogenic light-induced FT-IR difference spectra of the protein bacteriorhodopsin. The presence of these ghost bands can be particularly problematic in the 2800–1900 cm−1 region, showing intensities similar to O–D vibrations from water molecules…

0301 basic medicineMaterials scienceAbsorption spectroscopyInfraredAnalytical chemistryInfrared spectroscopy010402 general chemistry01 natural sciences03 medical and health sciencessymbols.namesakeSpectroscopy Fourier Transform InfraredFourier transform infrared spectroscopySpectroscopyInstrumentationSpectroscopybiologyProteinsBacteriorhodopsin0104 chemical sciences030104 developmental biologyApplied spectroscopyFourier transformBacteriorhodopsinssymbolsbiology.proteinArtifactsApplied Spectroscopy
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Assessing sensory versus optogenetic network activation by combining (o)fMRI with optical Ca2+ recordings

2016

Encoding of sensory inputs in the cortex is characterized by sparse neuronal network activation. Optogenetic stimulation has previously been combined with fMRI (ofMRI) to probe functional networks. However, for a quantitative optogenetic probing of sensory-driven sparse network activation, the level of similarity between sensory and optogenetic network activation needs to be explored. Here, we complement ofMRI with optic fiber-based population Ca2+ recordings for a region-specific readout of neuronal spiking activity in rat brain. Comparing Ca2+ responses to the blood oxygenation level-dependent signal upon sensory stimulation with increasing frequencies showed adaptation of Ca2+ transient…

0301 basic medicineGenetic VectorsPopulationOptogenetic fMRIChannelrhodopsinSensory systemStimulationOptogeneticsSomatosensory system03 medical and health sciences0302 clinical medicineChannelrhodopsinsTransduction GeneticBiological neural networkAnimalseducationEvoked PotentialsOptical FibersNeuronseducation.field_of_studyAniline CompoundsSensory stimulation therapyChemistrySomatosensory CortexOriginal Articlesoptical neurophysiologyFluoresceinsMagnetic Resonance ImagingRats Inbred F344calcium recordingsOptogeneticsOxygen030104 developmental biologyMicroscopy FluorescenceNeurologylight propagationCalciumFemalesparse network activationNeurology (clinical)Cardiology and Cardiovascular MedicineNeurosciencePhotic Stimulation030217 neurology & neurosurgeryJournal of Cerebral Blood Flow & Metabolism
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Probing a Polar Cluster in the Retinal Binding Pocket of Bacteriorhodopsin by a Chemical Design Approach

2012

Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C(13) of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoprotein…

Halobacterium salinarumModels MolecularProtein FoldingProtein Denaturation01 natural sciencesBiotecnologiaBiochemistryBiophysics Simulationschemistry.chemical_compoundSensory RhodopsinsHalobacterium salinarum0303 health sciencesMultidisciplinarybiologyProtein StabilityQRTemperatureUltraviolet-visible spectroscopyThermal stabilityBacterial BiochemistryChemistryBiochemistryBacteriorhodopsinsRetinaldehydeMedicineProtonsResearch ArticleSteric effectsHydrogen bondingBioquímicaProtein StructureScienceRetinal bindingBiophysics010402 general chemistryMicrobiologyPhosphates03 medical and health sciencesBiology030304 developmental biologyAspartic AcidBinding SitesAdaptation OcularOrganic ChemistryOrganic SynthesisProteinsChromoproteinsRetinalBacteriorhodopsinBacteriologyBiological TransportChromophorebiology.organism_classification0104 chemical sciencesTransmembrane ProteinschemistryRetinaldehydeBiophysicsbiology.proteinMutant ProteinsPLoS ONE
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Computational evidence in favor of a two-state, two-mode model of the retinal chromophore photoisomerization

2000

In this paper we use ab initio multiconfigurational second-order perturbation theory to establish the intrinsic photoisomerization path model of retinal chromophores. This is accomplished by computing the ground state ( S 0 ) and the first two singlet excited-state ( S 1 , S 2 ) energies along the rigorously determined photoisomerization coordinate of the rhodopsin chromophore model 4- cis -γ-methylnona-2,4,6,8-tetraeniminium cation and the bacteriorhodopsin chromophore model all- trans -hepta-2,4,6-trieniminium cation in isolated conditions. The computed S 2 and S 1 energy profiles do not show any avoided crossing feature along the S 1 reaction path and maintain an energy gap >20 kcal⋅…

PhotonsRhodopsinMultidisciplinaryPhotoisomerizationChemistryPhotochemistryAvoided crossingStatic ElectricityAb initioElectronic structureChromophoreMolecular physicsFluorescenceReaction coordinateIsomerismModels ChemicalComputational chemistryBacteriorhodopsinsPhysical SciencesAnimalsThermodynamicsComputer SimulationSinglet stateGround state
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