2008
Backbone structure of a small helical integral membrane protein: A unique structural characterization
Page RC, Lee S, Moore JD, Opella SJ, Cross TA. Backbone structure of a small helical integral membrane protein: A unique structural characterization. Protein Science 2008, 18: 134-146. PMID: 19177358, PMCID: PMC2708045, DOI: 10.1002/pro.24.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsSmall integral membrane proteinMembrane proteinsHelical integral membrane proteinsBackbone structureThree-dimensional backbone structureStructural characterizationTransmembrane helix proteinMembrane-mimetic environmentsAmino acid sequenceSolution NMR spectroscopyStructure determination approachChemical shift indexParamagnetic relaxation enhancementHelix proteinsTransmembrane domainExtramembranous domainsMembrane mimeticsMimetic environmentsStructural biologyDihedral restraintsGlobal foldAcid sequenceNMR spectroscopyOrientational restraints
2006
Comprehensive evaluation of solution nuclear magnetic resonance spectroscopy sample preparation for helical integral membrane proteins
Page RC, Moore JD, Nguyen HB, Sharma M, Chase R, Gao FP, Mobley CK, Sanders CR, Ma L, Sönnichsen FD, Lee S, Howell SC, Opella SJ, Cross TA. Comprehensive evaluation of solution nuclear magnetic resonance spectroscopy sample preparation for helical integral membrane proteins. Journal Of Structural And Functional Genomics 2006, 7: 51-64. PMID: 16850177, DOI: 10.1007/s10969-006-9009-9.Peer-Reviewed Original ResearchMeSH KeywordsCarbon IsotopesDetergentsEvaluation Studies as TopicMembrane ProteinsNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryConceptsHelical integral membrane proteinsIntegral membrane proteinsNuclear magnetic resonance spectroscopyMembrane proteinsStructural characterizationSolution nuclear magnetic resonance spectroscopyChemical shift correlation spectraRobust sample preparation methodSample preparationChemical shift correlationSolution NMR spectraSolution NMR spectroscopyShift correlation spectraSample preparation methodSample preparation protocolProper sample preparationEfficient purification protocolMagnetic resonance spectroscopyNMR spectroscopyShift correlationNMR spectraPreparation methodTransmembrane helicesResonance spectroscopyCorrelation spectra
2004
Functional Characterization and NMR Spectroscopy on Full-Length Vpu from HIV-1 Prepared by Total Chemical Synthesis
Kochendoerfer G, Jones D, Lee S, Oblatt-Montal M, Opella S, Montal M. Functional Characterization and NMR Spectroscopy on Full-Length Vpu from HIV-1 Prepared by Total Chemical Synthesis. Journal Of The American Chemical Society 2004, 126: 2439-2446. PMID: 14982452, DOI: 10.1021/ja038985i.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceHIV-1Human Immunodeficiency Virus ProteinsIon ChannelsLipid BilayersMicellesMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularRecombinant ProteinsViral Regulatory and Accessory ProteinsConceptsTotal chemical synthesisChemical synthesisNMR spectroscopyNative chemical ligation methodologyMembrane proteinsSolid-phase peptide synthesisSolid-state NMR spectraRecombinant proteinsPhase peptide synthesisSolution NMR spectroscopyFull-length VpuIntegral membrane proteinsHydrated lipid bilayerHomogeneous membrane proteinsLigation methodologyChemical ligationPeptide synthesisNMR spectraBacterial expressionFunctional characterizationSynthetic proteinsLipid micellesLipid bilayersCharacterization studiesOverall topology
2003
Structure and dynamics of a membrane protein in micelles from three solution NMR experiments
Lee S, Mesleh MF, Opella SJ. Structure and dynamics of a membrane protein in micelles from three solution NMR experiments. Journal Of Biomolecular NMR 2003, 26: 327-334. PMID: 12815259, DOI: 10.1023/a:1024047805043.Peer-Reviewed Original ResearchMeSH KeywordsAnisotropyCapsid ProteinsHydrophobic and Hydrophilic InteractionsMembrane ProteinsMicellesNuclear Magnetic Resonance, BiomolecularProtein ConformationSolutionsConceptsMembrane proteinsSolution NMR experimentsPISA wheelsLoop regionDipolar wavesResidual dipolar couplingsBackbone amide resonancesPf1 coat proteinHigh-throughput structural characterizationHeteronuclear NOE experimentsMembrane-bound formHydrophobic helicesHMQC-NOESY experimentsAmphipathic helixCoat proteinNMR experimentsMobile residuesHelical residuesBackbone dynamicsChemical shift anisotropyProteinAmide resonancesHelixResidual chemical shift anisotropyDipolar couplingsDipolar Waves Map the Structure and Topology of Helices in Membrane Proteins
Mesleh MF, Lee S, Veglia G, Thiriot DS, Marassi FM, Opella SJ. Dipolar Waves Map the Structure and Topology of Helices in Membrane Proteins. Journal Of The American Chemical Society 2003, 125: 8928-8935. PMID: 12862490, PMCID: PMC3272074, DOI: 10.1021/ja034211q.Peer-Reviewed Original ResearchMeSH KeywordsCapsid ProteinsMembrane ProteinsModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryReceptor, Muscarinic M2Receptors, MuscarinicConceptsMembrane proteinsDipolar wavesOrientation of helicesHelical membrane proteinsMolecular frameBilayer samplesMicelle samplesDipolar couplingsAbsolute rotationProteinHelixExperimental measurementsStructured residuesResiduesWavesStructure determinationNMR spectroscopyResidue numberSignificant stepRotationSpectroscopyWave mapsTurn periodCouplingKinksStructures of neuropeptide γ from goldfish and mammalian neuropeptide γ, as determined by 1H NMR spectroscopy
Lee K, Lee S, Kim Y, Park NG. Structures of neuropeptide γ from goldfish and mammalian neuropeptide γ, as determined by 1H NMR spectroscopy. Chemical Biology & Drug Design 2003, 61: 274-285. PMID: 12662361, DOI: 10.1034/j.1399-3011.2003.00058.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCircular DichroismGoldfishGuinea PigsMicellesNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein Structure, SecondarySodium Dodecyl SulfateSolutionsTachykininsConceptsAmino acid sequenceN-terminal regionAlpha-helical conformationAqueous TFE solutionAcid sequenceShort helixAlpha-helical structureC-terminal regionTerminal amino acid sequencePost-translational processingBeta-turn regionMammalian systemsTFE solutionC-terminusMet21Solution structureNeuropeptide γHelixBiological responsesGold fishBiological actionsSodium dodecyl sulfate micellesHis12Nuclear magnetic resonance spectroscopyNeuropeptide gamma
2000
Role of the Hinge Region and the Tryptophan Residue in the Synthetic Antimicrobial Peptides, Cecropin A(1−8)−Magainin 2(1−12) and Its Analogues, on Their Antibiotic Activities and Structures †, ‡
Oh D, Shin S, Lee S, Kang J, Kim S, Ryu P, Hahm K, Kim Y. Role of the Hinge Region and the Tryptophan Residue in the Synthetic Antimicrobial Peptides, Cecropin A(1−8)−Magainin 2(1−12) and Its Analogues, on Their Antibiotic Activities and Structures †, ‡. Biochemistry 2000, 39: 11855-11864. PMID: 11009597, DOI: 10.1021/bi000453g.Peer-Reviewed Original ResearchAmino Acid SequenceAmino Acid SubstitutionAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntineoplastic AgentsBacillus subtilisElectric ConductivityEscherichia coliHumansIon ChannelsJurkat CellsK562 CellsLipid BilayersMagaininsMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein Structure, SecondaryProtein Structure, TertiaryTryptophanXenopus Proteins
1999
Studies of the Chemical Structure of Gangliosides in Deer Antler, Cervus nippon
Jhon G, Park S, Han S, Lee S, Kim Y, Chang Y. Studies of the Chemical Structure of Gangliosides in Deer Antler, Cervus nippon. Chemical And Pharmaceutical Bulletin 1999, 47: 123. PMID: 9987834, DOI: 10.1248/cpb.47.123.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntlersCarbohydrate SequenceChromatography, High Pressure LiquidDeerG(M3) GangliosideGangliosidesGas Chromatography-Mass SpectrometryMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularConceptsHigh-field proton nuclear magnetic resonance spectroscopyFast atom bombardment mass spectrometry studiesProton nuclear magnetic resonance spectroscopyNuclear magnetic resonance spectroscopyGas chromatography/mass spectrometryChromatography/mass spectrometrySilica gel column chromatographyGel column chromatographyDirect compositional analysisDEAE-Sephadex AMagnetic resonance spectroscopyN-acetyl GM3Amperometric detectionChemical structurePrior derivatizationSpectrometry studiesStructural determinationTrifluoroacetic acidMass spectrometryResonance spectroscopyColumn chromatographyStandard monosaccharidesBiological activityStructure of gangliosidesCeramide moiety