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
1997
The effect of point mutations on the free energy of transmembrane α-helix dimerization11Edited by M. F. Moody
Fleming K, Ackerman A, Engelman D. The effect of point mutations on the free energy of transmembrane α-helix dimerization11Edited by M. F. Moody. Journal Of Molecular Biology 1997, 272: 266-275. PMID: 9299353, DOI: 10.1006/jmbi.1997.1236.Peer-Reviewed Original ResearchConceptsSodium dodecylsulfateVan der Waals interactionsAnalytical ultracentrifugationDer Waals interactionsFree energyMolecular association eventsEnergy of dimerizationOctyl etherWaals interactionsMolecular modelingRelative energy scaleDetergent environmentReversible associationEnergy differenceSedimentation equilibriumMonomersTransmembrane α-helicesNon-denaturing detergent solutionsDimer formationΑ-helixDimer stateAssociation eventsDetergent solutionDissociationHelix
1996
Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching
Adams P, Engelman D, Brünger A. Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching. Proteins Structure Function And Bioinformatics 1996, 26: 257-261. PMID: 8953647, DOI: 10.1002/(sici)1097-0134(199611)26:3<257::aid-prot2>3.0.co;2-b.Peer-Reviewed Original Research
1995
Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
Adams P, Arkin I, Engelman D, Brünger A. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nature Structural & Molecular Biology 1995, 2: 154-162. PMID: 7749920, DOI: 10.1038/nsb0295-154.Peer-Reviewed Original ResearchConceptsPentameric ion channelsTransmembrane domainThree-dimensional structureMembrane proteinsHydrophobic residuesΑ-helixIon channelsComputational searchingEnvironmental constraintsTwo-bodyGlobal searchPhospholambanMutagenesisComputational methodsHomopentamerProteinExperimental dataResiduesData yields