grant
Protein structure and dynamics in ultra-heterogeneous environments-Renewal
Organization UNIVERSITY OF TEXAS AT AUSTINLocation AUSTIN, UNITED STATESPosted 1 Aug 2019Deadline 31 May 2030
NIHUS FederalResearch GrantFY2025AddressAllergyArchitectureBioavailabilityBiologicalBiological AgentBiological AvailabilityBiological ProductsBuffersCell FunctionCell PhysiologyCell ProcessCellular FunctionCellular PhysiologyCellular ProcessComplexCrowdingCytosolDehydrationDiseaseDisorderElectrostaticsEngineering / ArchitectureEnvironmentEquilibriumH-bondHeterogeneityHydrogen BondingHydrogen OxideIlluminationIn SituKnowledgeLabelLightLightingLinkLiquid substanceMammalian CellMapsMeasurementMeasuresMembrane Protein GeneMembrane ProteinsMembrane-Associated ProteinsMicroscopicMolecularMolecular Modeling Nucleic Acid BiochemistryMolecular Modeling Protein/Amino Acid BiochemistryMolecular ModelsNon-Polyadenylated RNANucleic AcidsOligoOligonucleotidesPathway interactionsPhasePhotoradiationPhysical condensationPhysiologic AvailabilityPolymersPropertyProtein DynamicsProteinsRNARNA Gene ProductsResidualResidual stateRibonucleic AcidRoleSeriesSolventsSpinal ColumnSpineStructureSubcellular ProcessSurfaceSurface ProteinsTechniquesTherapeuticTranslatingVertebral columnWaterbackbonebalancebalance functionbiologicbiologicsbiopharmaceuticalbiotherapeutic agentbody water dehydrationcondensationcrosslinkdriving forcefluidimmunogenicityin vivoliquidmolecular modelingoligospathwaypolymerpolymericprotein oligomerprotein structureprotein structuresproteins structurepublic health relevancerational designsocial role
Description preview
SUMMARY
Hydrogen bonding in crowded environments – impact on biomolecules: Biomolecular organization in vivo
is driven by crowding and heterogeneity. To date, protein structure, dynamics, and folding have been studied
almost exclusively in buffer solutions, yet cellular environments are highly complex. This project seeks to
characterize the…
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