2010
Solution Structure and Phospholipid Interactions of the Isolated Voltage-Sensor Domain from KvAP
Butterwick JA, MacKinnon R. Solution Structure and Phospholipid Interactions of the Isolated Voltage-Sensor Domain from KvAP. Journal Of Molecular Biology 2010, 403: 591-606. PMID: 20851706, PMCID: PMC2971526, DOI: 10.1016/j.jmb.2010.09.012.Peer-Reviewed Original ResearchConceptsNuclear Overhauser effect spectroscopyNuclear magnetic resonance spectroscopySolution structureIsolated voltage-sensor domainBilayer-forming lipidsMagnetic resonance spectroscopyMicelle interactionsEffect spectroscopyChemical environmentCrystal structurePhospholipid interfaceChemical propertiesResonance spectroscopyPhospholipid micellesMembrane environmentPhospholipid bilayersNanosecond timescaleMillisecond timescaleMicellesSpectroscopyAmphipathic α-helixΑ-helixVoltage sensor domainRelaxation experimentsPhysical properties
2009
Pulsed Electron−Electron Double-Resonance Determination of Spin-Label Distances and Orientations on the Tetrameric Potassium Ion Channel KcsA
Endeward B, Butterwick JA, MacKinnon R, Prisner TF. Pulsed Electron−Electron Double-Resonance Determination of Spin-Label Distances and Orientations on the Tetrameric Potassium Ion Channel KcsA. Journal Of The American Chemical Society 2009, 131: 15246-15250. PMID: 19919160, PMCID: PMC2779547, DOI: 10.1021/ja904808n.Peer-Reviewed Original ResearchMeSH KeywordsBacteriaBacterial ProteinsElectron Spin Resonance SpectroscopyElectronsModels, MolecularMutationPotassium ChannelsProtein Structure, QuaternaryProtein Structure, TertiaryConceptsPELDOR dataElectron-electron double resonance measurementsTransverse spin relaxation timeProbe frequencySpin relaxation timeDouble resonance measurementsChannel KcsAMagnetic field strengthSpin-label distancesCentral channel axisPELDOR experimentsDetergent-solubilized samplesField strengthRelaxation timeOscillation frequencyResonance determinationQuantitative simulationChannel axisKcsAFrequencyOrientationMeasurementsAngle
2005
Solution Structure of the Vts1 SAM Domain in the Presence of RNA
Edwards TA, Butterwick JA, Zeng L, Gupta YK, Wang X, Wharton RP, Palmer AG, Aggarwal AK. Solution Structure of the Vts1 SAM Domain in the Presence of RNA. Journal Of Molecular Biology 2005, 356: 1065-1072. PMID: 16405996, DOI: 10.1016/j.jmb.2005.12.004.Peer-Reviewed Original ResearchConceptsSAM domainStructural basisCore helicesMultidimensional heteronuclear NMR spectroscopyRNA-binding surfaceSolution structureChemical shift perturbationsSpecific target RNAHeteronuclear NMR spectroscopyPresence of RNARNA bindingRNA recognitionC-terminusShift perturbationsTarget RNAShort helixMutational dataRNAHelix