2006
Mutations of Conserved Glycine Residues within the Membrane-Spanning Domain of Human Immunodeficiency Virus Type 1 gp41 Can Inhibit Membrane Fusion and Incorporation of Env onto Virions
Miyauchi K, Curran R, Matthews E, Komano J, Hoshino T, Engelman D, Matsuda Z. Mutations of Conserved Glycine Residues within the Membrane-Spanning Domain of Human Immunodeficiency Virus Type 1 gp41 Can Inhibit Membrane Fusion and Incorporation of Env onto Virions. Japanese Journal Of Infectious Diseases 2006, 59: 77-84. PMID: 16632906, DOI: 10.7883/yoken.jjid.2006.77.Peer-Reviewed Original Research
2001
The Cα—H⋅⋅⋅O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
Senes A, Ubarretxena-Belandia I, Engelman D. The Cα—H⋅⋅⋅O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 9056-9061. PMID: 11481472, PMCID: PMC55372, DOI: 10.1073/pnas.161280798.Peer-Reviewed Original ResearchConceptsMembrane protein structuresMembrane protein foldingTransmembrane helix associationTransmembrane helix interactionsHelix-helix interactionsTransmembrane helicesProtein foldingPacking interfaceHelix associationHelix interactionsProtein structureDeterminants of stabilityCalphaStructural motifsHelixSerineFoldingMotifHydrogen bondsImportant determinantInteractionGlycophorinSpecificityCαDeterminants
2000
Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions11Edited by G. von Heijne
Senes A, Gerstein M, Engelman D. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions11Edited by G. von Heijne. Journal Of Molecular Biology 2000, 296: 921-936. PMID: 10677292, DOI: 10.1006/jmbi.1999.3488.Peer-Reviewed Original ResearchAmino Acid MotifsAmino Acid SubstitutionAmino Acids, Branched-ChainBiasBinding SitesCell MembraneDatabases, FactualDimerizationGlycineGlycophorinsIsoleucineMathematicsMembrane ProteinsModels, MolecularMolecular WeightOdds RatioPliabilityProtein FoldingProtein Structure, SecondaryThermodynamicsValine
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