1994
Building a kinetic framework for group II intron ribozyme activity: quantitation of interdomain binding and reaction rate.
Pyle AM, Green JB. Building a kinetic framework for group II intron ribozyme activity: quantitation of interdomain binding and reaction rate. Biochemistry 1994, 33: 2716-25. PMID: 8117737, DOI: 10.1021/bi00175a047.Peer-Reviewed Original ResearchConceptsGeneral base catalysisChemical stepLinear rangeMichaelis-Menten mechanismSplice-site hydrolysisMultiple-turnover kinetic analysesPH/rate profileEnergetic stabilizationBase catalysisActive siteGel filtration chromatographyRibozyme kineticsReaction rateFiltration chromatographySpecific hydrolysisKinetic frameworkKinetic analysisHydrolysisReactionLower Km valuesBase pairingRibozyme activityKcat
1990
Direct measurement of oligonucleotide substrate binding to wild-type and mutant ribozymes from Tetrahymena.
Pyle AM, McSwiggen JA, Cech TR. Direct measurement of oligonucleotide substrate binding to wild-type and mutant ribozymes from Tetrahymena. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 8187-8191. PMID: 2236030, PMCID: PMC54920, DOI: 10.1073/pnas.87.21.8187.Peer-Reviewed Original ResearchConceptsSingle base changeBase-pairing interactionsGuanosine-binding siteRNA substratesSubstrate bindingRNA cleavageOligonucleotide substratesEfficient RNA cleavageTertiary interactionsBase changesRibozyme variantsTetrahymena ribozymeWeak substrateMutant ribozymesRibozymePolyacrylamide gelsEquilibrium dissociation constantsDeoxyribose sugarCatalytic activityDivalent cationsEnergetic stabilizationMutagenesisDissociation constantsTetrahymenaLow Mg2