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 ResearchConceptsMembrane 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
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