2000
Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: molecular dynamics calculations11Edited by G. Von Heijne
Petrache H, Grossfield A, MacKenzie K, Engelman D, Woolf T. Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: molecular dynamics calculations11Edited by G. Von Heijne. Journal Of Molecular Biology 2000, 302: 727-746. PMID: 10986130, DOI: 10.1006/jmbi.2000.4072.Peer-Reviewed Original ResearchMeSH Keywords1,2-DipalmitoylphosphatidylcholineAlgorithmsAmino Acid MotifsAmino Acid SequenceBinding SitesComputer SimulationDimerizationDimyristoylphosphatidylcholineGlycophorinsLipid BilayersModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide FragmentsPhosphatidylcholinesProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryThermodynamicsConceptsMonomer formLipid bilayersLipid chain lengthUnfavorable electrostatic repulsionLipid typeMolecular dynamics simulationsExplicit lipid bilayerElectrostatic repulsionMonomeric helicesLipid-lipid interactionsInteraction enthalpiesChain lengthDimer structureEnergetic propertiesCHARMM potentialInteraction energyAccessible volumeDynamics simulationsLipid propertiesUnsaturated lipidsEnthalpy calculationsLipid environmentBilayer thicknessAcyl chainsThermodynamic treatment
1996
Mapping the lipid-exposed surfaces of membrane proteins
Arkin I, MacKenzie K, Fisher L, Aimoto S, Engelman D, Smith S. Mapping the lipid-exposed surfaces of membrane proteins. Nature Structural & Molecular Biology 1996, 3: 240-243. PMID: 8605625, DOI: 10.1038/nsb0396-240.Peer-Reviewed Original ResearchConceptsMembrane proteinsLong transmembrane helixLipid-exposed surfaceThree-dimensional foldHigh-resolution structuresRelative rotational orientationTransmembrane helicesTransmembrane segmentsThird cysteineCysteine residuesLipid environmentHelix interfacePentameric complexProteinLipid interfaceStable complexesHelixResiduesUndergoes exchangeSulphydryl groupsPhospholambanComplexesInternal faceCysteineRotational orientation
1981
The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis
Engelman D, Steitz T. The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis. Cell 1981, 23: 411-422. PMID: 7471207, DOI: 10.1016/0092-8674(81)90136-7.Peer-Reviewed Original ResearchConceptsMembrane proteinsSecreted proteinsIntegral membrane proteinsHydrophobic leader peptideSecretion of proteinsHelical hairpinSpecific membrane receptorsPolypeptide sequenceSecond helixLeader peptideTransport proteinsLipid environmentTerminal helixN-terminusSpontaneous insertionMembrane receptorsHairpin structurePolypeptide structureProteinHelixHairpinHydrophobic interiorOnly alphaNonpolar sequencesHydrophobic portion