2012
ATP Utilization and RNA Conformational Rearrangement by DEAD-Box Proteins
Henn A, Bradley MJ, De La Cruz EM. ATP Utilization and RNA Conformational Rearrangement by DEAD-Box Proteins. Annual Review Of Biophysics 2012, 41: 247-267. PMID: 22404686, PMCID: PMC7761782, DOI: 10.1146/annurev-biophys-050511-102243.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsDEAD-box RNA HelicasesHumansKineticsMolecular Motor ProteinsNucleic Acid ConformationRNAThermodynamicsConceptsDEAD-box proteinsNucleotide-dependent interactionRegulatory partner proteinsMolecular motor proteinsMolecular motor functionPartner proteinsRNA helicasesHelicase coreRNA helicaseRNA metabolismVivo foldingATP bindingDBP functionMotor proteinsCellular RNARNA structureQuantitative mechanistic understandingConformational rearrangementsBiophysical investigationsEnzymatic adaptationLarge familyMechanistic understandingProteinRNAAuxiliary domain
2007
Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates
Zhang H, Cao W, Zakharova E, Konigsberg W, De La Cruz EM. Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates. Nucleic Acids Research 2007, 35: 6052-6062. PMID: 17766250, PMCID: PMC2094073, DOI: 10.1093/nar/gkm587.Peer-Reviewed Original ResearchConceptsHydroxyl groupsNucleotidyl transfer reactionMinimal kinetic schemeConformational changesDetectable fluorescence changeChemical quenchTransfer reactionsDependent fluorescence enhancementFluorescence enhancementFluorescence quenchingFluorescent probeRapid conformational changesTemplate complexN-positionRate constantsFluorescence changesRapid fluorescenceTernary complexKinetic schemeComplexesTemplating baseDependent conformational changesDp/TTemplateFluorescence