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
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 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
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