1991
Interactions of the A1 heterogeneous nuclear ribonucleoprotein and its proteolytic derivative, UP1, with RNA and DNA: evidence for multiple RNA binding domains and salt-dependent binding mode transitions.
Nadler S, Merrill B, Roberts W, Keating K, Lisbin M, Barnett S, Wilson S, Williams K. Interactions of the A1 heterogeneous nuclear ribonucleoprotein and its proteolytic derivative, UP1, with RNA and DNA: evidence for multiple RNA binding domains and salt-dependent binding mode transitions. Biochemistry 1991, 30: 2968-76. PMID: 1848781, DOI: 10.1021/bi00225a034.Peer-Reviewed Original ResearchAmino Acid SequenceCircular DichroismDNA HelicasesDNA-Binding ProteinsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsKineticsMolecular Sequence DataNucleic Acid DenaturationPoly A-UPoly dA-dTPolydeoxyribonucleotidesPolyribonucleotidesRibonucleoproteinsSpectrometry, FluorescenceThermodynamicsThymus Hormones[25] Identification of amino acid residues at interface of protein—Nucleic acid complexes by photochemical cross-linking
Williams K, Konigsberg W. [25] Identification of amino acid residues at interface of protein—Nucleic acid complexes by photochemical cross-linking. Methods In Enzymology 1991, 208: 516-539. PMID: 1779846, DOI: 10.1016/0076-6879(91)08027-f.Peer-Reviewed Original ResearchAdenosine TriphosphateAnimalsBinding SitesChromatography, High Pressure LiquidChromatography, Ion ExchangeColiphagesCross-Linking ReagentsDNADNA-Binding ProteinsElectrophoresis, Polyacrylamide GelEscherichia coliHumansKineticsOligodeoxyribonucleotidesPeptide FragmentsPhosphorus RadioisotopesPhotochemistryPolydeoxyribonucleotidesProtein BindingRadioisotope Dilution Technique
1990
Purification and functional characterization of adenovirus ts111A DNA-binding protein. Fluorescence studies of protein-nucleic acid binding.
Meyers M, Keating K, Roberts W, Williams K, Chase J, Horwitz M. Purification and functional characterization of adenovirus ts111A DNA-binding protein. Fluorescence studies of protein-nucleic acid binding. Journal Of Biological Chemistry 1990, 265: 5875-5882. PMID: 2318838, DOI: 10.1016/s0021-9258(19)39444-x.Peer-Reviewed Original Research
1979
T4 gene 32 protein trypsin-generated fragments. Fluorescence measurement of DNA-binding parameters.
Spicer E, Williams K, Konigsberg W. T4 gene 32 protein trypsin-generated fragments. Fluorescence measurement of DNA-binding parameters. Journal Of Biological Chemistry 1979, 254: 6433-6436. PMID: 221499, DOI: 10.1016/s0021-9258(18)50385-9.Peer-Reviewed Original Research
1978
Structural changes in the T4 gene 32 protein induced by DNA polynucleotides.
Williams K, Konigsberg W. Structural changes in the T4 gene 32 protein induced by DNA polynucleotides. Journal Of Biological Chemistry 1978, 253: 2463-2470. PMID: 632279, DOI: 10.1016/s0021-9258(17)38096-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino AcidsCarrier ProteinsColiphagesDNA, ViralGenes, ViralKineticsPeptide FragmentsPolydeoxyribonucleotidesViral ProteinsConceptsGene 32 proteinT4 gene 32 proteinDNA-binding proteinsT4 DNA metabolismTryptic hydrolysisPartial trypsin digestionDNA metabolismGene 32Protein interactionsBacteriophage T4COOH terminusNH2 terminusLimited tryptic hydrolysisCooperative bindingDNA complexesDNA interactionAmino acidsProteinTrypsin digestionDNA polynucleotidesConformational probeTerminusDalton fragmentFragmentsHydrolysis