2014
Conformational Preferences Underlying Reduced Activity of a Thermophilic Ribonuclease H
Stafford KA, Trbovic N, Butterwick JA, Abel R, Friesner RA, Palmer AG. Conformational Preferences Underlying Reduced Activity of a Thermophilic Ribonuclease H. Journal Of Molecular Biology 2014, 427: 853-866. PMID: 25550198, PMCID: PMC4349505, DOI: 10.1016/j.jmb.2014.11.023.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCrystallography, X-RayEscherichia coliHot TemperatureHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular Dynamics SimulationMutationNuclear Magnetic Resonance, BiomolecularPrincipal Component AnalysisProtein BindingProtein ConformationRibonuclease HThermodynamicsThermus thermophilusConceptsE. coli homologWild-type proteinRibonuclease HE. coli mutantsGlycine-rich regionMesophilic homologsThermophilus enzymeColi mutantsSubstrate bindingThermophilic proteinsImportant residuesThermus thermophilusConformational dynamicsGlycine residueMesophilic enzymesActive conformationLoop regionAtom MD simulationsConformational basisReduced activityEscherichia coliHomologProteinPosition 80MD simulations
2006
An inserted Gly residue fine tunes dynamics between mesophilic and thermophilic ribonucleases H
Butterwick JA, Palmer AG. An inserted Gly residue fine tunes dynamics between mesophilic and thermophilic ribonucleases H. Protein Science 2006, 15: 2697-2707. PMID: 17088323, PMCID: PMC2242442, DOI: 10.1110/ps.062398606.Peer-Reviewed Original ResearchConceptsRNase HConformational changesGly residueMesophile Escherichia coliThermophile Thermus thermophilusSolution NMR spectroscopyIntrahelical hydrogen bondsHomologous mesophilicProtein sequencesBiological functionsThermus thermophilusImportant adaptationGly insertionPutative hingeEscherichia coliRibonuclease HMesophilicResiduesDynamic processUnfavorable interactionsThermophilesThermophilicProteinNMR spectroscopyThermophilus