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 ResearchConceptsHelical 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 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
Dipolar 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 ResearchConceptsMembrane proteinsDipolar wavesOrientation of helicesHelical membrane proteinsMolecular frameBilayer samplesMicelle samplesDipolar couplingsAbsolute rotationProteinHelixExperimental measurementsStructured residuesResiduesWavesStructure determinationNMR spectroscopyResidue numberSignificant stepRotationSpectroscopyWave mapsTurn periodCouplingKinks
1999
Comparison of the Structures of β Amyloid Peptide (25–35) and Substance P in Trifluoroethanol/Water Solution
Lee S, Suh Y, Kim S, Kim Y. Comparison of the Structures of β Amyloid Peptide (25–35) and Substance P in Trifluoroethanol/Water Solution. Journal Of Biomolecular Structure And Dynamics 1999, 17: 381-391. PMID: 10563586, DOI: 10.1080/07391102.1999.10508369.Peer-Reviewed Original ResearchConceptsSubstance PTrifluoroethanol/water solutionTachykinin familyAmyloid peptidesBrains of patientsHydrophobic side chainsBeta-amyloid peptideNMR spectroscopyAqueous solutionΒ-amyloid peptideAlpha-helical structureAromatic ringConformational featuresWater solutionSide chainsTachykinin receptorsBeta amyloidSenile plaquesAlzheimer's diseaseThree-dimensional structureDiseaseReceptors