Search results for "Biophysics Simulations"

showing 5 items of 5 documents

Structural Mechanism of N-Methyl-D-Aspartate Receptor Type 1 Partial Agonism

2012

N-methyl-D-aspartate (NMDA) receptors belong to a family of ionotropic glutamate receptors that contribute to the signal transmission in the central nervous system. NMDA receptors are heterotetramers that usually consist of two GluN1 and GluN2 monomers. The extracellular ligand-binding domain (LBD) of a monomer is comprised of discontinuous segments that form the functional domains D1 and D2. While the binding of a full agonist glycine to LBD of GluN1 is linked to cleft closure and subsequent ion-channel opening, partial agonists are known to activate the receptor only sub-maximally. Although the crystal structures of the LBD of related GluA2 receptor explain the mechanism for the partial a…

AgonistProtein Structuremedicine.drug_classGlycineMolecular ConformationBiophysicslcsh:MedicineMolecular Dynamics SimulationLigandsta3111Receptors N-Methyl-D-AspartateBiochemistryBiophysics Simulationsta3112Partial agonistIon ChannelsChemical BiologyMacromolecular Structure AnalysismedicineBiomacromolecule-Ligand Interactionslcsh:ScienceReceptorBiologyta116Ion channelCrystallographyMultidisciplinaryChemistrylcsh:Rta1182Glutamate receptorProteinsComputational BiologyNeurotransmittersProtein Structure TertiaryTransmembrane ProteinsBiochemistryCycloserineBiophysicsNMDA receptorLigand-gated ion channellcsh:Qhormones hormone substitutes and hormone antagonistsProtein BindingResearch ArticleNeuroscienceIonotropic effectPLoS ONE
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Protein diffusion in mammalian cell cytoplasm.

2011

We introduce a new method for mesoscopic modeling of protein diffusion in an entire cell. This method is based on the construction of a three-dimensional digital model cell from confocal microscopy data. The model cell is segmented into the cytoplasm, nucleus, plasma membrane, and nuclear envelope, in which environment protein motion is modeled by fully numerical mesoscopic methods. Finer cellular structures that cannot be resolved with the imaging technique, which significantly affect protein motion, are accounted for in this method by assigning an effective, position-dependent porosity to the cell. This porosity can also be determined by confocal microscopy using the equilibrium distribut…

Fluorescence-lifetime imaging microscopyCytoplasmMass diffusivity01 natural sciencesBiophysics Simulationslaw.inventionDiffusionlawMolecular Cell BiologyImage Processing Computer-Assistedprotein diffusionMammals0303 health sciencesMultidisciplinaryMicroscopy ConfocalChemistrysolulimaPhysicsQRCell biologyMedicineproteiinin diffuusioPorosityFluorescence Recovery After PhotobleachingResearch ArticleScienceCellsBiophysicsFluorescence correlation spectroscopyModels Biological03 medical and health sciencesdiffuusio (fysikaaliset ilmiöt)Bacterial ProteinsConfocal microscopy0103 physical sciencesAnimalsHumansComputer Simulation010306 general physicsBiology030304 developmental biologyNucleoplasmProtein transportta114ta1182Fluorescence recovery after photobleachingProteinsReproducibility of ResultssoluPhotobleachingProteiinien kuljetusLuminescent ProteinsMicroscopy FluorescenceCytoplasmCatsCellHeLa CellsPloS one
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CO rebinding kinetics and molecular dynamics simulations highlight dynamic regulation of internal cavities in human cytoglobin

2013

Abstract: Cytoglobin (Cygb) was recently discovered in the human genome and localized in different tissues. It was suggested to play tissue-specific protective roles, spanning from scavenging of reactive oxygen species in neurons to supplying oxygen to enzymes in fibroblasts. To shed light on the functioning of such versatile machinery, we have studied the processes supporting transport of gaseous heme ligands in Cygb. Carbon monoxide rebinding shows a complex kinetic pattern with several distinct reaction intermediates, reflecting rebinding from temporary docking sites, second order recombination, and formation (and dissociation) of a bis-histidyl heme hexacoordinated reaction intermediate…

Genetics and Molecular Biology (all)ProteomicsProtein FoldingProtein ConformationMolecular biologylcsh:MedicineCrystallography X-RayLigandsBiophysics SimulationsBiochemistrychemistry.chemical_compoundProtein structureMacromolecular Structure AnalysisCinètica enzimàticaBinding Sites; Carbon Monoxide; Crystallography X-Ray; Globins; Humans; Kinetics; Ligands; Molecular Dynamics Simulation; Oxygenases; Point Mutation; Protein Binding; Protein Conformation; Medicine (all); Biochemistry Genetics and Molecular Biology (all); Agricultural and Biological Sciences (all)Biomacromolecule-Ligand Interactionslcsh:ScienceHemeCarbon MonoxideCrystallographyHemoproteinsMultidisciplinaryMedicine (all)PhysicsCytoglobinMetabolismeGlobinsBiochemistryOxygenasesddc:500Engineering sciences. TechnologyProtein BindingResearch ArticleBioquímicaProtein StructureBiophysicsReaction intermediateMolecular Dynamics SimulationProtein ChemistryGeneticsHumansPoint MutationGlobinProtein InteractionsBiologyBiologia molecularBinding SitesLigandCytoglobinlcsh:REnzyme kineticsOxygen transportProteinsComputational BiologyKineticsMetabolismAgricultural and Biological Sciences (all)chemistryX-RayBiophysicslcsh:QHuman medicineGenèticaCarbon monoxide
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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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Conformational changes in acetylcholine binding protein investigated by temperature accelerated molecular dynamics.

2014

Despite the large number of studies available on nicotinic acetylcholine receptors, a complete account of the mechanistic aspects of their gating transition in response to ligand binding still remains elusive. As a first step toward dissecting the transition mechanism by accelerated sampling techniques, we study the ligand-induced conformational changes of the acetylcholine binding protein (AChBP), a widely accepted model for the full receptor extracellular domain. Using unbiased Molecular Dynamics (MD) and Temperature Accelerated Molecular Dynamics (TAMD) simulations we investigate the AChBP transition between the apo and the agonist-bound state. In long standard MD simulations, both confo…

Nicotinic Acetylcholine ReceptorsProtein ConformationGatingMolecular DynamicsLigandsBiochemistryBiophysics SimulationsIon ChannelsMolecular dynamicsAcetylcholine bindingComputational ChemistryBiochemical SimulationsNicotinic AgonistsBiomacromolecule-Ligand InteractionsBiochemistry SimulationsMultidisciplinaryHydrogen bondChemistryPhysicsQTemperatureRLigand (biochemistry)nicotinic receptor molecular dynamics tamd acethylcholine binding proteinChemistryNicotinic agonistBiochemistryMedicineBiophysic Al SimulationsResearch ArticleProtein BindingProtein subunitScienceBiophysicsMolecular Dynamics SimulationProtein ChemistryStatistical MechanicsChemical BiologyAnimalsBiologyAcetylcholine receptorBinding SitesProteinsComputational BiologyHydrogen BondingSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein SubunitsMolluscaAcetylcholine ReceptorsBiophysicsLobelineCarrier ProteinsPLoS ONE
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