2001
Use of EPR Spectroscopy to Study Macromolecular Structure and Function
Biswas R, KÜhne H, Brudvig G, Gopalan V. Use of EPR Spectroscopy to Study Macromolecular Structure and Function. Science Progress 2001, 84: 45-68. PMID: 11382137, PMCID: PMC10367463, DOI: 10.3184/003685001783239050.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonance spectroscopyProtein-nucleic acid complexesSpin-labeling reagentParamagnetic resonance spectroscopySpin labelsEPR spectroscopyAcid complexesBiological macromoleculesEPR spectraSite-specific substitutionMacromolecular structureResonance spectroscopyNucleic acidsSpectroscopyRecent applicationsStructural aspectsCommercial availabilityMacromoleculesCysteine residuesReagentsAdvent of techniquesStructure-function correlatesExperimental strategiesComplexesPowerful tool
1999
Mapping RNA−Protein Interactions in Ribonuclease P from Escherichia coli Using Electron Paramagnetic Resonance Spectroscopy †
Gopalan V, Kühne H, Biswas R, Li H, Brudvig G, Altman S. Mapping RNA−Protein Interactions in Ribonuclease P from Escherichia coli Using Electron Paramagnetic Resonance Spectroscopy †. Biochemistry 1999, 38: 1705-1714. PMID: 10026248, DOI: 10.1021/bi9807106.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBinding SitesComputer SimulationElectron Spin Resonance SpectroscopyEndoribonucleasesEscherichia coliEscherichia coli ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein FoldingRibonuclease PRibonucleoproteinsRNA, BacterialRNA, CatalyticSpin LabelsStructure-Activity RelationshipConceptsM1 RNAC5 proteinRibonuclease PCysteine residuesEscherichia coliRNA-protein interfaceCatalytic RNA subunitNative cysteine residuesSulfhydryl-specific reagentsCatalytic ribonucleoproteinRNA subunitHoloenzyme complexRNP complexesProtein cofactorsMutant derivativesDeletion derivativesRNASpin labelsProteinSpectroscopy-based approachRibonucleoproteinResiduesPosition 16Coli