Midwest Center for Membrane Protein Structural Dynamics
中西部膜蛋白结构动力学中心
基本信息
- 批准号:7498602
- 负责人:
- 金额:$ 7.68万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2008
- 资助国家:美国
- 起止时间:2008-03-01 至 2010-02-28
- 项目状态:已结题
- 来源:
- 关键词:ATP phosphohydrolaseAcetylcholineActive SitesAddressAlgorithmsAmino AcidsAmyloid beta-Protein PrecursorAnisotropyAntibodiesApplied GeneticsArchaeaArchitectureAreaArtsAssesAttentionAwardBacteriaBacteriorhodopsinsBaculovirusesBehaviorBindingBinding ProteinsBiochemicalBiochemical ReactionBiochemistryBiogenesisBiologicalBiological ProcessBiologyBiomassBiophysicsCatalysisCell NucleusCellsChargeChemicalsChemistryChicagoChildhoodChromosome PairingClassClassificationCodeCollaborationsCommunicationCommunitiesComplementComplexComputational algorithmComputing MethodologiesConditionConsensusContractsCopperCore FacilityCouplesCouplingCrystallizationCrystallographyCytokine ReceptorsDNADNA SequenceDNA Sequence RearrangementDataDatabasesDecompression SicknessDenmarkDetergentsDeteriorationDevelopmentDisciplineDiseaseDisease AssociationDrosophila genusDrug DesignDyesEcologyEcosystemElectron Spin Resonance SpectroscopyElectron TransportElectronsElectrophysiology (science)ElementsEnd PointEndopeptidasesEndpoint DeterminationEnergy TransferEnergy-Generating ResourcesEngineeringEnvironmentEquilibriumEventEvolutionFamilyFigs - dietaryFluorescenceFluorescence MicroscopyFluorescence Resonance Energy TransferFluorescence SpectroscopyFogsFosteringFourier TransformFree EnergyFreedomFundingGated Ion ChannelGene AmplificationGene ExpressionGene ProteinsGenerationsGeneticGenomeGenomicsGoalsGrantGrowthHealthHeartHeavy MetalsHistidineHomeostasisHormonesHourHumanHuman GeneticsHuman GenomeHybridsHydrolysisIllinoisImageIndividualInfectionInsectaInstitutesInstitutionIntegral Membrane ProteinInternetInvestigationInvestmentsIon ChannelIonsIsotope LabelingKidneyKnockout MiceKnowledgeLabelLaboratoriesLanthanoid Series ElementsLeadLeadershipLengthLibrariesLibrary ServicesLifeLiftingLigand BindingLigandsLinkLiposomesLiquid substanceLocationMacromolecular ComplexesMagnetic ResonanceMammalian CellMapsMeasurableMeasurementMeasuresMediatingMembraneMembrane BiologyMembrane PotentialsMembrane ProteinsMembrane Structure and FunctionMeta-AnalysisMetagenomicsMetalsMethionineMethodologyMethodsMicroscopicModelingModificationMolecularMolecular BiologyMolecular ChaperonesMolecular ConformationMolecular GeneticsMolecular MachinesMolecular WeightMolecular and Cellular BiologyMonitorMotionMovementMultienzyme ComplexesMuscleMutagenesisMyosin ATPaseNMR SpectroscopyNa(+)-K(+)-Exchanging ATPaseNatureNerveNeurobiologyNeurotransmitter ReceptorNoiseNuclearNuclear Magnetic ResonanceNuclear ReceptorsNumbersOligonucleotidesOocytesOperative Surgical ProceduresOptical MethodsOpticsOrganismOxygenPTEN genePanthera oncaParticipantPathway interactionsPediatricsPeptide HydrolasesPeptidesPerformancePhage DisplayPharmacologyPhasePhosphatidylinositolsPhosphoric Monoester HydrolasesPhysical ChemistryPhysicsPhysiologic pulsePhysiological ProcessesPhysiologyPlanetsPlayPolymerase Chain ReactionPositioning AttributePost-Translational Protein ProcessingPotassium ChannelPreparationPrincipal InvestigatorProcessProductionProlactin ReceptorPropertyProtein AnalysisProtein BiochemistryProtein BiosynthesisProtein ConformationProtein DynamicsProtein EngineeringProtein RegionProteinsProteolysisProteomePsychological TechniquesPublishingPulse takingPumpPurple MembranePurposeRangeRateReactionReagentReceptor ActivationRegulationRelative (related person)RelaxationReporterReportingResearchResearch InfrastructureResearch InstituteResearch PersonnelResolutionResource AllocationResourcesRetinalRhodopsinRoentgen RaysRoleSamplingScaffolding ProteinScienceScreening procedureSecondary toSecureSeriesSerineServicesShapesSideSignal PathwaySignal TransductionSimulateSiteSite-Directed MutagenesisSkeletal MuscleSolidSolutionsSolventsSomatotropinSourceSpecific qualifier valueSpectroscopy, Fourier Transform InfraredSpectrum AnalysisSpeedSpin LabelsStagingStandards of Weights and MeasuresStatistical MechanicsStimulusStreamStructural ProteinStructureSupport of ResearchSurfaceSynapsesSynaptic TransmissionSystemSystems BiologyTechniquesTechnologyTerbiumTertiary Protein StructureTestingTimeTravelUnited States National Institutes of HealthUniversitiesVertebral columnWaterWeightWorkX-Ray CrystallographyYeastsamyloid precursor protein processinganticancer researchaqueousbasecell growthcell motilitychemical additionchemical bondchemical synthesiscombinatorialcomputer studiescomputerized toolsconceptconformational conversioncovalent bondcytokinedaydensitydesigndesign and constructionelectric fieldelectrical measurementelectron donorexpectationexperiencefeedingimprovedin vivoinnovationinsightinterestligand gated channelluminescence resonance energy transfermacromoleculemagnetic fieldmembermetagenomic sequencingmicrobial communitymicroorganismmilligrammillisecondmolecular dynamicsmolecular recognitionmultidisciplinarymutantnanodevicenanomachinenanosecondnitroxylnovelnovel strategiesparallel computingparticlepatch clamppeptide chemical synthesisphosphorescencepresenilin-1programsprotein expressionprotein foldingprotein functionprotein protein interactionprotein purificationprotein structurequantumquantum chemistryreceptorreceptor functionreconstitutionresearch studyresponserhomboidscaffoldsecretasesensorsimulationsingle moleculesteroid hormonestructural biologystructural genomicssuccesstetramethylrhodaminetheoriesthree dimensional structuretooltraffickingvoltagevoltage gated channelwater channelyeast two hybrid system
项目摘要
DESCRIPTION (provided by applicant): Membrane proteins play an essential role in controlling the movement of material and information in and out of the cell, in determining the flow and use of energy, as well as in triggering the initiation of numerous signaling pathways. To fulfill these roles, conformational and interaction dynamics exert a dominant influence on their functional behavior, for it is the interplay between structure and dynamics what ultimately defines their function. The Midwest Center for Membrane Protein Structural Dynamics (MMPSD) is proposed as a highly interactive, tightly integrated and multidisciplinary effort focused on elucidating the relationship between structure, free energy landscapes, dynamics and function.
The MMPSD will be organized around multidisciplinary project teams with investigators from institutions clustered geographically inn [sic] the Midwest to maximize true interactive collaborations and an efficient exchange of ideas. These teams will study major mechanistic questions associated with membrane protein function as it relates to three major areas: energy transduction in signaling (ion channels and receptors) energy interconversion (transporters and pumps) and chemo-transduction pathways (membrane-embedded proteases and phosphatases). Our ultimate goals is to decode the general mechanistic principles that govern protein movement and its associated fluctuation dynamics by dissecting and analyzing the molecular and dynamical bases of these functions at an unprecedented and quantitative level, as well as exploiting this information to engineer altered and novel activities into membrane protein frameworks to rationally evolve new functions. To accomplish its goals, the MMPSD will develop in parallel a set of tools, concepts and reagents to: 1) Determine time-averaged structures of "Archetype" membrane proteins using Chaperone-assisted crystallization methods; 2) Apply state of the art spectroscopic methods (Magnetic Resonance, Fluorescence) to follow conformational changes and dynamics of the determined structures; and 3) Design and implement novel computational approaches to link static and dynamic data with function. Four core facilities will feed and interconnect with the individual projects in a highly interactive way. The cores will support the research in the Center by providing service and expertise in four critical areas: Membrane protein expression, the establishment of chemical synthesis capabilities for probes and detergents, the generation of a large variety of crystallization chaperones and other target binders, and generation of a pipeline of novel membrane targets through metagenomics approaches.
All of the information, tools and new reagents/targets will be shared with the research community at large through the "membrane protein dynamics gateway", a state of the art web page and a series of scientific meetings open to the public.
描述(由申请人提供):膜蛋白在控制物质和信息进出细胞的运动,决定能量的流动和使用以及触发许多信号通路的启动方面起着至关重要的作用。为了完成这些角色,构象动力学和相互作用动力学对它们的功能行为施加了主要影响,因为结构和动力学之间的相互作用最终决定了它们的功能。中西部膜蛋白结构动力学中心(MMPSD)是一个高度互动,紧密集成和多学科的努力,专注于阐明结构,自由能景观,动力学和功能之间的关系。
项目成果
期刊论文数量(1)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Eduardo A Perozo其他文献
Eduardo A Perozo的其他文献
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{{ truncateString('Eduardo A Perozo', 18)}}的其他基金
Structural Basis of Coupling and Dynamics in K+ Channels
K 通道耦合和动力学的结构基础
- 批准号:
10682241 - 财政年份:2023
- 资助金额:
$ 7.68万 - 项目类别:
Structural basis of Outer Hair Cell Electromotility at High Resolution
高分辨率外毛细胞电动性的结构基础
- 批准号:
10317974 - 财政年份:2021
- 资助金额:
$ 7.68万 - 项目类别:
Structural basis of Outer Hair Cell Electromotility at High Resolution
高分辨率外毛细胞电动性的结构基础
- 批准号:
10625831 - 财政年份:2021
- 资助金额:
$ 7.68万 - 项目类别:
Structural basis of Outer Hair Cell Electromotility at High Resolution
高分辨率外毛细胞电动性的结构基础
- 批准号:
10416073 - 财政年份:2021
- 资助金额:
$ 7.68万 - 项目类别:
Structural Basis of “Force from Lipids” Activation in Mechanosensitive Channels
机械敏感通道中“脂质力”激活的结构基础
- 批准号:
10454805 - 财政年份:2019
- 资助金额:
$ 7.68万 - 项目类别:
Structural Basis of “Force from Lipids” Activation in Mechanosensitive Channels
机械敏感通道中“脂质力”激活的结构基础
- 批准号:
9766038 - 财政年份:2019
- 资助金额:
$ 7.68万 - 项目类别:
Structural Basis of “Force from Lipids” Activation in Mechanosensitive Channels
机械敏感通道中“脂质力”激活的结构基础
- 批准号:
10216309 - 财政年份:2019
- 资助金额:
$ 7.68万 - 项目类别:
STRUCTURAL BASIS FOR K+ CHANNEL SLOW INACTIVATION
K 通道缓慢失活的结构基础
- 批准号:
8169261 - 财政年份:2010
- 资助金额:
$ 7.68万 - 项目类别:
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