2013
Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics
Xia S, Wood M, Bradley MJ, De La Cruz EM, Konigsberg WH. Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics. Nucleic Acids Research 2013, 41: 9077-9089. PMID: 23921641, PMCID: PMC3799440, DOI: 10.1093/nar/gkt674.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionCatalytic DomainDeoxyribonucleotidesDNADNA-Directed DNA PolymeraseExodeoxyribonucleasesFluorescence Resonance Energy TransferKineticsModels, MolecularProtein ConformationThymine NucleotidesViral ProteinsConceptsRB69 DNA polymeraseFörster resonance energy transferDNA polymeraseHigh-resolution X-ray crystallographyResolution X-ray crystallographyHigh mutation rateB-family polConformational dynamicsExonuclease domainState kinetic parametersMutation rateG mutantResonance energy transferX-ray crystallographyM variantPolymerasePrimer terminusHydrophobic cavityActive siteBase selectivitySimilar substitutionSide chainsProfound effectDramatic effectInternal cavity
2005
Thymosin β4 Induces a Conformational Change in Actin Monomers
Dedova IV, Nikolaeva OP, Safer D, De La Cruz EM, dos Remedios CG. Thymosin β4 Induces a Conformational Change in Actin Monomers. Biophysical Journal 2005, 90: 985-992. PMID: 16272441, PMCID: PMC1367123, DOI: 10.1529/biophysj.105.063081.Peer-Reviewed Original ResearchAcrylamideActinsAdenosine TriphosphateAnimalsCalorimetry, Differential ScanningCysteineElectrophoresis, Polyacrylamide GelFluorescence Resonance Energy TransferHot TemperatureKineticsLysineModels, MolecularMolecular ConformationNucleotidesProtein BindingProtein ConformationProtein Structure, TertiaryPurinesRabbitsSolventsSpectrometry, FluorescenceTemperatureThymosin