2007
NMR and mutagenesis of human copper transporter 1 (hCtr1) show that Cys-189 is required for correct folding and dimerization
Lee S, Howell SB, Opella SJ. NMR and mutagenesis of human copper transporter 1 (hCtr1) show that Cys-189 is required for correct folding and dimerization. Biochimica Et Biophysica Acta 2007, 1768: 3127-3134. PMID: 17959139, PMCID: PMC2275670, DOI: 10.1016/j.bbamem.2007.08.037.Peer-Reviewed Original ResearchMeSH KeywordsCation Transport ProteinsCloning, MolecularCopper Transporter 1CysteineDimerizationElectrophoresis, Polyacrylamide GelHumansMagnetic Resonance SpectroscopyModels, BiologicalModels, GeneticProtein FoldingConceptsMembrane proteinsHuman high-affinity copper transporterHigh-affinity copper transporterCys-189Polytopic membrane proteinsSolution-state NMR methodsMetal-binding motifHuman copper transporter 1Site-directed mutagenesisCopper transporter 1Cys-161Transmembrane helicesExperimental structure determinationProper foldingCorrect foldingCopper transporterCysteine residuesBinding motifProteinDimer formationMutagenesisTransporter 1FoldingStructure determinationNMR methods
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 ResearchMeSH KeywordsHistidineMagnetic Resonance SpectroscopyMicellesModels, ChemicalModels, MolecularNeurokinin BPhenylalanineProtein ConformationProtein Structure, TertiarySodium Dodecyl SulfateTrifluoroethanolTryptophanConceptsNuclear 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 drugsResiduesProtonsComparison 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 ResearchMeSH KeywordsAmyloid beta-PeptidesCircular DichroismComputer SimulationMagnetic Resonance SpectroscopyPeptide FragmentsProtein Structure, SecondaryProtein Structure, TertiarySubstance PTrifluoroethanolWaterConceptsSubstance 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