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
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 ResearchConceptsTotal 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 ResearchConceptsMembrane 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 couplingsStructures 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 ResearchConceptsAmino 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
1999
Solution structure of neuromedin B by 1H nuclear magnetic resonance spectroscopy
Lee S, Kim Y. Solution structure of neuromedin B by 1H nuclear magnetic resonance spectroscopy. FEBS Letters 1999, 460: 263-269. PMID: 10544247, DOI: 10.1016/s0014-5793(99)01346-0.Peer-Reviewed Original ResearchConceptsNuclear magnetic resonance spectroscopySDS micellesMagnetic resonance spectroscopyTwo-dimensional nuclear magnetic resonance spectroscopyResonance spectroscopyAromatic ring protonsSolution structureMembrane-mimicking environmentHydrophobic acyl chainsStructure-activity relationshipsMethylene protonsLongitudinal relaxation dataNOESY experimentsHelical conformationConformational featuresRing protonsMicellesMolecular mechanismsSpectroscopyAcyl chainsExtrinsic interactionsRelaxation dataEfficient drugsResiduesProtons