1992
Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster
Shuai K, Gupta C, Hawley R, Chase J, Stone K, Williams K. Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster. Nucleic Acids Research 1992, 20: 1379-1385. PMID: 1313969, PMCID: PMC312186, DOI: 10.1093/nar/20.6.1379.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino AcidsAnimalsChromatography, DEAE-CelluloseChromatography, High Pressure LiquidDNA, Single-StrandedDrosophila melanogasterElectrophoresis, Polyacrylamide GelEndonucleasesExonucleasesHot TemperatureHydrogen-Ion ConcentrationKineticsMolecular Sequence DataMolecular WeightSodium ChlorideSubstrate SpecificityUltracentrifugationShuffling of amino acid sequence: an important control in synthetic peptide studies of nucleic acid-binding domains. Binding properties of fragments of a conserved eukaryotic RNA binding motif.
Nadler S, Kapouch J, Elliott J, Williams K. Shuffling of amino acid sequence: an important control in synthetic peptide studies of nucleic acid-binding domains. Binding properties of fragments of a conserved eukaryotic RNA binding motif. Journal Of Biological Chemistry 1992, 267: 3750-3757. PMID: 1740426, DOI: 10.1016/s0021-9258(19)50589-0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCarrier ProteinsCircular DichroismFungal ProteinsGenes, FungalHot TemperatureMolecular Sequence DataNucleic Acid DenaturationNucleic AcidsPeptide FragmentsPoly APoly A-UPoly(A)-Binding ProteinsRNA, FungalRNA-Binding ProteinsSaccharomyces cerevisiaeSpectrometry, FluorescenceSubstrate SpecificityConceptsNucleic acidsPeptide studiesResidue peptideSynthetic peptide studiesSynthetic peptidesSynthetic peptide analoguesFree energyProperties of fragmentsPeptide analoguesNucleic acid-binding domainParent proteinLatter peptideNucleic acid bindingAmino acidsStructure/function studiesAmino acid sequenceSignificant affinityAcidEukaryotic RNAPeptidesRNA specificityAmino acid compositionSimilar RNACarboxyl halfMolecular basis
1984
Characterization of the structural and functional defect in the Escherichia coli single-stranded DNA binding protein encoded by the ssb-1 mutant gene. Expression of the ssb-1 gene under lambda pL regulation.
Williams K, Murphy J, Chase J. Characterization of the structural and functional defect in the Escherichia coli single-stranded DNA binding protein encoded by the ssb-1 mutant gene. Expression of the ssb-1 gene under lambda pL regulation. Journal Of Biological Chemistry 1984, 259: 11804-11811. PMID: 6384214, DOI: 10.1016/s0021-9258(20)71283-4.Peer-Reviewed Original ResearchConceptsWild-type SSBMutant proteinsSSB-1Solid-phase protein sequencingSsb-1 mutationSSB-1 proteinHelix-destabilizing proteinNormal cellular concentrationTryptic peptide analysisSubstitution of tyrosineSingle-strand DNAProtein sequencingDNA sequencesMutant geneResidues 55Thermal melting transitionCellular concentrationTemperature inductionTetrameric structureEscherichia coliProteinGenesProtein concentrationPeptide analysisT transition