2001
Computation and mutagenesis suggest a right‐handed structure for the synaptobrevin transmembrane dimer
Fleming K, Engelman D. Computation and mutagenesis suggest a right‐handed structure for the synaptobrevin transmembrane dimer. Proteins Structure Function And Bioinformatics 2001, 45: 313-317. PMID: 11746678, DOI: 10.1002/prot.1151.Peer-Reviewed Original ResearchConceptsTransmembrane dimerSingle transmembrane segmentBiological membrane fusionProtein-protein interactionsRight-handed structureInterhelical hydrogen bondsSequence-specific mannerTransmembrane segmentsDimerization motifThree-dimensional structureMutagenesis studiesMembrane fusionSuccessful structure predictionSide-chain atomsStructure predictionSpecific mannerKey playersComputational searchDimersSynaptobrevinMutagenesisComputational methodsAssociation thermodynamicsMotifGlycophorin
1997
A Transmembrane Helix Dimer: Structure and Implications
MacKenzie K, Prestegard J, Engelman D. A Transmembrane Helix Dimer: Structure and Implications. Science 1997, 276: 131-133. PMID: 9082985, DOI: 10.1126/science.276.5309.131.Peer-Reviewed Original ResearchConceptsMembrane-spanning alpha helicesSolution nuclear magnetic resonance spectroscopyDimeric transmembrane domainNuclear magnetic resonance spectroscopyTransmembrane helix dimerVan der Waals interactionsDer Waals interactionsAqueous detergent micellesIntermonomer hydrogen bondsTransmembrane helicesTransmembrane domainMagnetic resonance spectroscopyThree-dimensional structureDetergent micellesHelix dimerHydrogen bondsWaals interactionsAlpha-helixResonance spectroscopyGlycophorin ASpecific associationHelixSequence dependenceMicellesSpectroscopy
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
1990
The "microassembly" of integral membrane proteins: applications & implications.
Popot J, Engelman D, Zaccai G, de Vitry C. The "microassembly" of integral membrane proteins: applications & implications. Progress In Clinical And Biological Research 1990, 343: 237-62. PMID: 2198582.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsMembrane proteinsFunctional integral membrane proteinsMost integral membrane proteinsSingle transmembrane alpha-helixInner membrane complexTransmembrane alpha-helixAutonomous folding domainsInner membraneIntegral subunitThree-dimensional structureTransmembrane regionSequence dataMembrane complexAlpha-helixExtensive rearrangementTertiary structureProteinPolypeptideLipid phasePossible roleOrganellesBiosynthesisSubunitsLocal interactions
1984
Neutron Scattering and the 30 S Ribosomal Subunit of E. coli
Moore P, Engelman D, Langer J, Ramakrishnan V, Schindler D, Schoenborn B, Sillers I, Yabuki S. Neutron Scattering and the 30 S Ribosomal Subunit of E. coli. Basic Life Sciences 1984, 27: 73-91. PMID: 6370225, DOI: 10.1007/978-1-4899-0375-4_4.Peer-Reviewed Original Research