1997
Assessment of the aggregation state of integral membrane proteins in reconstituted phospholipid vesicles using small angle neutron scattering11Edited by M. F. Moody
Hunt J, McCrea P, Zaccaı̈ G, Engelman D. Assessment of the aggregation state of integral membrane proteins in reconstituted phospholipid vesicles using small angle neutron scattering11Edited by M. F. Moody. Journal Of Molecular Biology 1997, 273: 1004-1019. PMID: 9367787, DOI: 10.1006/jmbi.1997.1330.Peer-Reviewed Original ResearchConceptsMembrane protein complexesIntegral membrane proteinsProtein complexesMembrane proteinsIntegral membrane protein complexPhospholipid vesiclesSmall unilamellar phospholipid vesiclesUnilamellar phospholipid vesiclesMolecular massF. MoodySpatial arrangementNon-ionic detergentIndividual complexesVesiclesModel systemMonomeric bacteriorhodopsinProteinUnknown scopeComplexesAggregation stateRadius of gyrationBacteriorhodopsinDetergentsBilayers
1996
Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban
Ludlam C, Arkin I, Liu X, Rothman M, Rath P, Aimoto S, Smith S, Engelman D, Rothschild K. Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban. Biophysical Journal 1996, 70: 1728-1736. PMID: 8785331, PMCID: PMC1225141, DOI: 10.1016/s0006-3495(96)79735-7.Peer-Reviewed Original ResearchConceptsSite-directed isotope labelingLocal secondary structureIsotope labelingSecondary structureSelective ion channelsTotal reflection Fourier transformPeptide amide groupsAmide IReflection Fourier transformDeuterium/hydrogen exchangeTransmembrane domainMembrane domainsMembrane proteinsTransmembrane orientationAmino acid fragmentSpectroscopic characterizationIon channelsHydrophobic regionAmide carbonylProtein backboneCardiac muscle cellsAmide groupLipid bilayersATPase activityFourier transform
1983
Neutron diffraction analysis of cytochrome b5 reconstituted in deuterated lipid multilayers
Gogol E, Engelman D, Zaccai G. Neutron diffraction analysis of cytochrome b5 reconstituted in deuterated lipid multilayers. Biophysical Journal 1983, 43: 285-292. PMID: 6626669, PMCID: PMC1329297, DOI: 10.1016/s0006-3495(83)84352-5.Peer-Reviewed Original Research
1979
[51] Neutron-scattering measurement of protein pair scattering functions from ribosomes containing deuterated proteins
Engelman D. [51] Neutron-scattering measurement of protein pair scattering functions from ribosomes containing deuterated proteins. Methods In Enzymology 1979, 59: 656-669. PMID: 440090, DOI: 10.1016/0076-6879(79)59120-4.Peer-Reviewed Original Research
1976
Protein pair distance determination in the 30 S ribosomal subunit of E. coli.
Engelman D, Moore P, Schoenborn B. Protein pair distance determination in the 30 S ribosomal subunit of E. coli. Brookhaven Symposia In Biology 1976, iv20-iv37. PMID: 786445.Peer-Reviewed Original ResearchThe production of deuterated E. coli.
Moore P, Engelman D. The production of deuterated E. coli. Brookhaven Symposia In Biology 1976, v12-v23. PMID: 786448.Peer-Reviewed Original Research
1975
Determination of Quaternary Structure by Small Angle Neutron Scattering
Engelman D, Moore P. Determination of Quaternary Structure by Small Angle Neutron Scattering. Annual Review Of Biophysics And Bioengineering 1975, 4: 219-241. PMID: 1098555, DOI: 10.1146/annurev.bb.04.060175.001251.Peer-Reviewed Original Research
1974
Asymmetry in the 50S Ribosomal Subunit of Escherichia coli
Moore P, Engelman D, Schoenborn B. Asymmetry in the 50S Ribosomal Subunit of Escherichia coli. Proceedings Of The National Academy Of Sciences Of The United States Of America 1974, 71: 172-176. PMID: 4589891, PMCID: PMC387959, DOI: 10.1073/pnas.71.1.172.Peer-Reviewed Original Research
1972
A New Method for the Determination of Biological Quarternary Structure by Neutron Scattering
Engelman D, Moore P. A New Method for the Determination of Biological Quarternary Structure by Neutron Scattering. Proceedings Of The National Academy Of Sciences Of The United States Of America 1972, 69: 1997-1999. PMID: 4506067, PMCID: PMC426853, DOI: 10.1073/pnas.69.8.1997.Peer-Reviewed Original Research
1971
Structural comparisons of native and reaggregated membranes from Mycoplasma laidlawii and erythrocytes by X-ray diffraction and nuclear magnetic resonance techniques
Metcalfe J, Metcalfe S, Engelman D. Structural comparisons of native and reaggregated membranes from Mycoplasma laidlawii and erythrocytes by X-ray diffraction and nuclear magnetic resonance techniques. Biochimica Et Biophysica Acta 1971, 241: 412-421. PMID: 5159791, DOI: 10.1016/0005-2736(71)90041-1.Peer-Reviewed Original ResearchMeSH KeywordsAcetoneAcholeplasma laidlawiiAlcoholsBacterial ProteinsBenzyl CompoundsBinding SitesCell MembraneCentrifugation, Density GradientChemical PrecipitationDetergentsDeuteriumDialysisErythrocytesLipidsMacromolecular SubstancesMagnetic Resonance SpectroscopyMicroscopy, ElectronMycoplasmaSulfatesUltracentrifugationX-Ray DiffractionConceptsRelaxation measurementsMagnetic relaxation measurementsNuclear magnetic relaxation measurementsNuclear magnetic resonance techniquesNative membranesProbe experimentsX-ray diffraction patternsX-ray diffractionMagnetic resonance techniquesSodium dodecyl sulfateLipid bilayer structureProbe techniqueProbe moleculesBenzyl alcoholResonance techniquesDiffraction patternsBilayer regionsDodecyl sulfateBilayer structureElectron microscopyMembrane systemStructural comparisonMeasurementsMembraneDiffractionStructural comparisons of native and reaggregated membranes from Mycoplasma laidlawii and erythrocytes using a fluorescence probe
Metcalfe S, Metcalfe J, Engelman D. Structural comparisons of native and reaggregated membranes from Mycoplasma laidlawii and erythrocytes using a fluorescence probe. Biochimica Et Biophysica Acta 1971, 241: 422-430. PMID: 5159792, DOI: 10.1016/0005-2736(71)90042-3.Peer-Reviewed Original Research