1996
Matrix-Assisted Laser Desorption Ionization Mass Spectrometry as a Complement to Internal Protein Sequencing
Williams K, Samandar S, Stone K, Saylor M, Rush J. Matrix-Assisted Laser Desorption Ionization Mass Spectrometry as a Complement to Internal Protein Sequencing. Springer Protocols Handbooks 1996, 541-555. DOI: 10.1007/978-1-60327-259-9_91.Peer-Reviewed Original ResearchLaser desorption ionization mass spectrometryDesorption ionization mass spectrometryIonization mass spectrometryMass spectrometryMatrix-Assisted Laser Desorption Ionization Mass SpectrometryInternal protein sequencingBiological moleculesMALDI-MSSimple instrumentationSpectrometryBiochemical laboratoryMass analysis methodProtein sequencingMoleculesHigh throughput
1985
Identification of a nucleic acid helix-destabilizing protein from rat liver as lactate dehydrogenase-5.
Williams K, Reddigari S, Patel G. Identification of a nucleic acid helix-destabilizing protein from rat liver as lactate dehydrogenase-5. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 5260-5264. PMID: 2991914, PMCID: PMC390547, DOI: 10.1073/pnas.82.16.5260.Peer-Reviewed Original ResearchConceptsHelix-destabilizing proteinSs-DNAAmino acid compositionHPLC tryptic peptide mapsNucleic acid helix-destabilizing proteinSolid-phase protein sequencingChemical modification studiesCoenzyme binding siteTyrosine-238Molecular weightSimilar amino acid compositionsTryptic peptide mapsAcid compositionLactate dehydrogenase 5Molecular homogeneitySimilar specific activitiesProtein sequencingLDH proteinDNA bindingAmino terminusBiological roleSingle proteinM chainTryptic peptidesVivo role
1984
Bacteriophage T4 gene 44 DNA polymerase accessory protein. Sequences of gene 44 and its protein product.
Spicer E, Nossal N, Williams K. Bacteriophage T4 gene 44 DNA polymerase accessory protein. Sequences of gene 44 and its protein product. Journal Of Biological Chemistry 1984, 259: 15425-15432. PMID: 6096371, DOI: 10.1016/s0021-9258(17)42566-x.Peer-Reviewed Original ResearchConceptsGene 44DNA polymerase accessory proteinEscherichia coli RNA polymeraseT4 middle genesT4 DNA replicationAmino acidsPolymerase accessory proteinsPotential regulatory regionsColi RNA polymeraseDirect protein sequencingT4-infected cellsTranslation initiation regionRegA proteinMiddle genesSequence similarityAmino acid compositionDNA replicationRNA polymeraseRegulatory regionsProtein sequencingAccessory proteinsDNA sequencesNucleotide sequenceProtein sequencesNucleotides 5Characterization 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