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Receptors, ProgesteroneCell MembraneMembrane ProteinsProgesteroneProtein Structure, TertiaryMembranesMembrane LipidsIntracellular MembranesMembrane PotentialsMembranes, ArtificialErythrocyte MembraneBacterial Outer Membrane ProteinsMembrane FluidityCell Membrane PermeabilityBasement MembraneMembrane Transport ProteinsMolecular Sequence DataAmino Acid SequenceMembrane GlycoproteinsLipid BilayersProtein TransportDetergentsEscherichia coliBacterial ProteinsProtein BindingMicroscopy, ElectronCell LineElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumMitochondrial MembranesCarrier ProteinsMutationGolgi ApparatusMolecular WeightModels, BiologicalLiposomesRecombinant Fusion ProteinsCell FractionationBase SequenceSynaptic MembranesPorinsModels, MolecularProtein ConformationEscherichia coli ProteinsProtein Structure, SecondaryCloning, MolecularCalciumSolubilityCells, CulturedMicroscopy, FluorescenceSequence Homology, Amino AcidHydrogen-Ion ConcentrationViral Matrix ProteinsSubcellular FractionsBinding SitesPhosphatidylcholinesCytoplasmRecombinant ProteinsFreeze FracturingTemperatureFluorescent Antibody TechniqueEndocytosisRabbitsErythrocytesProtein Sorting SignalsMicroscopy, ImmunoelectronMitochondriaKineticsExtraembryonic MembranesBlotting, WesternCattleBiological Transport, ActiveMicroscopy, ConfocalMicrovilliEndosomesTime FactorsPeptidesIon ChannelsSignal TransductionLysosome-Associated Membrane GlycoproteinsVacuolesCricetinaeImmunoblottingCell Membrane StructuresSaccharomyces cerevisiae ProteinsHydrophobic and Hydrophilic InteractionsOctoxynolTransfectionPurple MembraneCytosolMicellesProtein Processing, Post-TranslationalPotassiumAdenosine TriphosphateGreen Fluorescent ProteinsNuclear EnvelopeReceptors, Cell SurfaceMicrosomesDiffusionExocytosis
LipidsNational InstitutCrystallizationStructure InitiativeGeneStructuresDomainsMultiple
Lipids2
  • Proteins that cross the membrane are surrounded by annular lipids, which are defined as lipids that are in direct contact with a membrane protein. (wikipedia.org)
  • Type V proteins are anchored to the lipid bilayer through covalently linked lipids. (wikipedia.org)
National Institut1
  • The Protein Structure Initiative (PSI), funded by the U.S. National Institute of General Medical Sciences (NIGMS), part of the National Institutes of Health (NIH), has among its aim to determine three-dimensional protein structures and to develop techniques for use in structural biology, including for membrane proteins. (wikipedia.org)
Crystallization2
  • Their membrane-anchoring α-helices have been removed to facilitate the extraction and crystallization. (wikipedia.org)
  • As in the past, topics of gene cloning, gene expression, protein purification and crystallization and rapid NMR structure determination were highlighted in the meeting program. (nih.gov)
Structure Initiative2
  • Improvements in methodology and technology to permit the more rapid, less expensive and more predictable determination of the structure of protein targets remains a major goal of the NIGMS Protein Structure Initiative (PSI). (nih.gov)
  • Dr. John Norvell, director of the PSI, introduced the workshop and discussed the current progress and the future of the PSI program particularly in the context of the recent evaluation of the Protein Structure Initiative by representatives of the National Advisory General Medical Sciences Council. (nih.gov)
Gene1
  • Search integral membrane proteins in the PDB (based on gene ontology classification) IMPs can be divided into two groups: Integral polytopic proteins (Transmembrane proteins) Integral monotopic proteins The most common type of IMP is the transmembrane protein (TM), which spans the entire biological membrane. (wikipedia.org)
Structures2
Domains2
  • Type III proteins have multiple transmembrane domains in a single polypeptide, while type IV consists of several different polypeptides assembled together in a channel through the membrane. (wikipedia.org)
  • Finally Type VI proteins have both transmembrane domains and lipid anchors. (wikipedia.org)
Multiple1
  • Proteins that bind PI typically have two motifs (or multiple motifs) which allow for temporal and spatial separation of binding events. (nih.gov)