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
1989
Site-specific mutagenesis of T4 gene 32: the role of tyrosine residues in protein-nucleic acid interactions.
Shamoo Y, Ghosaini L, Keating K, Williams K, Sturtevant J, Konigsberg W. Site-specific mutagenesis of T4 gene 32: the role of tyrosine residues in protein-nucleic acid interactions. Biochemistry 1989, 28: 7409-17. PMID: 2684276, DOI: 10.1021/bi00444a039.Peer-Reviewed Original ResearchMeSH KeywordsCalorimetry, Differential ScanningCircular DichroismDNA, Single-StrandedDNA, ViralDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelEscherichia coliGene Expression RegulationGenes, ViralMutationNucleic Acid DenaturationPoly dA-dTPoly TProtein DenaturationTemperatureThermodynamicsT-PhagesTrypsinTyrosineViral ProteinsZinc
1987
The function of zinc in gene 32 protein from T4.
Giedroc D, Keating K, Williams K, Coleman J. The function of zinc in gene 32 protein from T4. Biochemistry 1987, 26: 5251-9. PMID: 3314985, DOI: 10.1021/bi00391a007.Peer-Reviewed Original Research
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 transitionCharacterization of the Escherichia coli SSB-113 mutant single-stranded DNA-binding protein. Cloning of the gene, DNA and protein sequence analysis, high pressure liquid chromatography peptide mapping, and DNA-binding studies.
Chase J, L'Italien J, Murphy J, Spicer E, Williams K. Characterization of the Escherichia coli SSB-113 mutant single-stranded DNA-binding protein. Cloning of the gene, DNA and protein sequence analysis, high pressure liquid chromatography peptide mapping, and DNA-binding studies. Journal Of Biological Chemistry 1984, 259: 805-814. PMID: 6363409, DOI: 10.1016/s0021-9258(17)43529-0.Peer-Reviewed Original Research