1999
Identification of the RNA Binding Domain of T4 RegA Protein by Structure-based Mutagenesis*
Gordon J, Sengupta T, Phillips C, O'Malley S, Williams K, Spicer E. Identification of the RNA Binding Domain of T4 RegA Protein by Structure-based Mutagenesis*. Journal Of Biological Chemistry 1999, 274: 32265-32273. PMID: 10542265, DOI: 10.1074/jbc.274.45.32265.Peer-Reviewed Original ResearchConceptsRegA proteinBeta-sheet residuesGel mobility shift assaysRNA gel mobility shift assaysProtein-RNA interactionsMutagenesis of residuesRNA Binding DomainRNA binding siteMobility shift assaysRNA recognition propertiesBeta-sheet regionUnique structural motifMutant proteinsRNA bindingProtein foldsShift assaysBinding domainsMutagenesis studiesStructural domainsDomain IIMutagenesisEquilibrium binding assaysProteinRNABinding sites
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
1982
Comparative Peptide Mapping by HPLC: Identification of Single Amino Acid Substitutions in Temperature Sensitive Mutants
Williams K, L’Italien J, Guggenheimer R, Sillerud L, Spicer E, Chase J, Konigsberg W. Comparative Peptide Mapping by HPLC: Identification of Single Amino Acid Substitutions in Temperature Sensitive Mutants. Experimental Biology And Medicine 1982, 499-507. DOI: 10.1007/978-1-4612-5832-2_44.Peer-Reviewed Original ResearchPeptide mappingChemical modificationCovalent proteinComparative peptide mappingAmino acid analysisProtein structureParticular amino acid replacementsPrimary structureLac repressor moleculesHuman hemoglobinHPLCAcid analysisSubstitutionStructurePowerful approachSingle amino acid substitutionCrosslinkingMoleculesAmino acid substitutionsSubtitutionAcid substitutionsMutant proteins