1992
Identification of amino acid residues at the interface of a bacteriophage T4 regA protein-nucleic acid complex.
Webster K, Keill S, Konigsberg W, Williams K, Spicer E. Identification of amino acid residues at the interface of a bacteriophage T4 regA protein-nucleic acid complex. Journal Of Biological Chemistry 1992, 267: 26097-26103. PMID: 1464621, DOI: 10.1016/s0021-9258(18)35722-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBacteriophage T4Base SequenceBinding SitesChromatography, High Pressure LiquidCross-Linking ReagentsMolecular Sequence DataOligoribonucleotidesPeptide FragmentsPlasmidsPromoter Regions, GeneticRNA, MessengerRNA, ViralSequence Homology, Amino AcidTrypsinUltraviolet RaysConceptsCross-linked peptidesProtein-nucleic acid complexesAnion-exchange high-performance liquid chromatographyNucleic acidsIntact proteinHigh-performance liquid chromatographyCross-linked complexGas-phase sequencingPerformance liquid chromatographyAcid complexesExchange high performance liquid chromatographyLiquid chromatographyChemical cleavageBacteriophage T4 regA proteinNucleic acid bindingTryptic peptidesComplexesUltraviolet lightCNBr peptidesPeptidesCN6Amino acid residuesMeasurable affinityAcid bindingAcidPurification 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 SpecificityUltracentrifugationElution and Internal Amino Acid Sequencing of PVDF-Blotted Proteins
Stone K, LoPresti M, Williams K, Mcnulty D, Crawford J, DeAngelis R. Elution and Internal Amino Acid Sequencing of PVDF-Blotted Proteins. 1992, 23-34. DOI: 10.1016/b978-0-12-058756-8.50008-0.Peer-Reviewed Original ResearchPVDF membranePolyacrylamide gel electrophoresisPolyvinylidene difluoride membraneTryptic digestMolecular weightReversed-phase HPLCSDS-polyacrylamide gel electrophoresisHigh yieldsTotal purificationDifluoride membraneEnzymatic cleavageTryptic peptidesPhase HPLCCyanogen bromide peptidesCyanogen bromide cleavageCleavageInternal amino acid sequencingGel electrophoresisPeptidesAmino acid sequencingMembraneElutionPurification
1991
Amino Acid Analysis and Sequencing — What is State-of-the-Art?
Niece R, Ericsson L, Fowler A, Smith A, Speicher D, Crabb J, Williams K. Amino Acid Analysis and Sequencing — What is State-of-the-Art? Advances In Life Sciences 1991, 133-141. DOI: 10.1007/978-3-0348-5678-2_12.Peer-Reviewed Original Research
1990
Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain.
Kumar A, Widen S, Williams K, Kedar P, Karpel R, Wilson S. Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain. Journal Of Biological Chemistry 1990, 265: 2124-2131. PMID: 2404980, DOI: 10.1016/s0021-9258(19)39949-1.Peer-Reviewed Original ResearchConceptsNH2-terminal domainDNA polymerase betaLarge-scale overproductionPolymerase betaMammalian DNA polymerase betaCOOH-terminal domainProtease-sensitive regionNucleic acidsProteolysis experimentsRat proteinRecombinant proteinsPolypeptide chainDNA polymerase activityIntact proteinEscherichia coliAmino acidsTryptic peptidesDNA polymeraseDomain structureProteinPolymerase activityDomainPolymeraseAcidDNA[21] Reversed-phase high-performance liquid chromatography for fractionation of enzymatic digests and chemical cleavage products of proteins
Stone K, Elliott J, Peterson G, McMurray W, Williams K. [21] Reversed-phase high-performance liquid chromatography for fractionation of enzymatic digests and chemical cleavage products of proteins. Methods In Enzymology 1990, 193: 389-412. PMID: 2074828, DOI: 10.1016/0076-6879(90)93429-o.Peer-Reviewed Original ResearchConceptsHigh-performance liquid chromatographyReversed-phase high-performance liquid chromatographyReversed phase high performance liquid chromatographyLiquid chromatographyEnzymatic digestsHigh peak capacityMass spectrometric approachProtein chemistsSpectrometric approachMass spectrometryPeak capacityComplex mixturesMolecular weightChemical cleavageGradient timeCleavage productsChromatographyTryptic peptidesPeptidesDigestsChemistsSpectrometryFractionationProductsPrimary structure
1988
Phenylalanines that are conserved among several RNA-binding proteins form part of a nucleic acid-binding pocket in the A1 heterogeneous nuclear ribonucleoprotein.
Merrill B, Stone K, Cobianchi F, Wilson S, Williams K. Phenylalanines that are conserved among several RNA-binding proteins form part of a nucleic acid-binding pocket in the A1 heterogeneous nuclear ribonucleoprotein. Journal Of Biological Chemistry 1988, 263: 3307-3313. PMID: 2830282, DOI: 10.1016/s0021-9258(18)69073-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCarrier ProteinsCattleChromatography, AffinityChromatography, High Pressure LiquidDNA HelicasesDNA, Single-StrandedElectrophoresis, Polyacrylamide GelHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataNucleic AcidsPeptide FragmentsPhenylalaninePhenylthiohydantoinPhotochemistryPoly TRatsRibonucleoproteinsRNA-Binding ProteinsSerine EndopeptidasesThymus HormonesTrypsinConceptsRNA-binding proteinHeterogeneous nuclear ribonucleoproteinsA1 heterogeneous nuclear ribonucleoproteinNuclear ribonucleoproteinRepeat sequencesPhenylalanine residuesRNA-binding pocketDNA-cellulose chromatographyInternal repeat sequencesStaphylococcus aureus VSequence homologyCovalent adduct formationA1 proteinPrimary structurePartial proteolysisAnalogous positionsAmino acidsTryptic peptidesProteinPolypeptideProteolytic fragmentsRibonucleoproteinFirst experimental evidenceResiduesCellulose chromatographyPhotochemical crosslinking of bacteriophage T4 single‐stranded DNA‐binding protein (gp32) to oligo‐p(dT)8: Identification of phenylalanine‐183 as the site of crosslinking
Shamoo Y, Williams K, Konigsberg W. Photochemical crosslinking of bacteriophage T4 single‐stranded DNA‐binding protein (gp32) to oligo‐p(dT)8: Identification of phenylalanine‐183 as the site of crosslinking. Proteins Structure Function And Bioinformatics 1988, 4: 1-6. PMID: 3186689, DOI: 10.1002/prot.340040103.Peer-Reviewed Original ResearchConceptsCovalent bond formationAnion-exchange high-performance liquid chromatographyHigh-performance liquid chromatographyBond formationGas-phase sequencingLiquid chromatographyPhotochemical crosslinkingPhenylthiohydantoin derivativesSer-GlyTryptic peptidesUltraviolet irradiationTyr-AspUltraviolet lightCrosslinkingSer-AsnHigh affinityCleavage productsGln-ValGlu-SerPeptidesPhotolysisTrypsin cleavage productSingle tryptic peptideChromatographyComplexes
1987
Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking.
Pandey V, Williams K, Stone K, Modak M. Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking. Biochemistry 1987, 26: 7744-8. PMID: 3322406, DOI: 10.1021/bi00398a031.Peer-Reviewed Original ResearchConceptsCross-linking reactionReversed-phase high-performance liquid chromatographyHigh-performance liquid chromatographyCross-linking sitesEscherichia coli DNA polymerase IPeptide lossKlenow fragmentChelate formLiquid chromatographyAmino acid analysisE. coli DNA Pol ISmall peptidesTryptic digestionSubstrate deoxynucleoside triphosphateHistidine residuesTryptic peptidesAmino acidsSingle peptideOptimal conditionsPeptide mappingDNA Pol IStaphylococcus aureus V8 protease digestionDNA polymerase IAcceptor sitesPeptides
1985
Amino acid sequence of the UP1 calf thymus helix-destabilizing protein and its homology to an analogous protein from mouse myeloma.
Williams K, Stone K, LoPresti M, Merrill B, Planck S. Amino acid sequence of the UP1 calf thymus helix-destabilizing protein and its homology to an analogous protein from mouse myeloma. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 5666-5670. PMID: 2994041, PMCID: PMC390612, DOI: 10.1073/pnas.82.17.5666.Peer-Reviewed Original ResearchConceptsAmino acid sequenceAmino acidsAnalogous proteinsAcid sequenceHelix-destabilizing proteinsComplete amino acid sequenceHelix-destabilizing proteinStaphylococcus aureus V8 proteaseSimilar amino acidsAureus V8 proteaseMouse proteinCyanogen bromide cleavageMouse sequencesProtein sequencesSequence homologyCOOH terminusNH2 terminusSolid-phase sequencingGas-phase sequencingV8 proteaseEndoproteinase LysTryptic peptidesProteinUP1Calf thymusIdentification 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
1981
Primary structure of the bacteriophage T4 DNA helix-destabilizing protein.
Williams K, LoPresti M, Setoguchi M. Primary structure of the bacteriophage T4 DNA helix-destabilizing protein. Journal Of Biological Chemistry 1981, 256: 1754-1762. PMID: 6257686, DOI: 10.1016/s0021-9258(19)69872-8.Peer-Reviewed Original ResearchConceptsGene 32 proteinT4 DNA replication proteinsPrimary structureDNA replication proteinsDNA-binding proteinsHelix-destabilizing proteinLimited trypsin digestionGene 32Replication proteinsUnusual stretchesSerine residuesCyanogen bromide cleavageBacteriophage T4DNA bindingSequencing of peptidesAlpha-helixTyrosine residuesBeta sheetNative proteinStaphylococcal proteaseCooperative bindingAmino acidsTryptic peptidesPosition 72Protein
1980
Amino acid sequence of the T4 DNA helix-destabilizing protein.
Williams K, LoPresti M, Setoguchi M, Konigsberg W. Amino acid sequence of the T4 DNA helix-destabilizing protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 4614-4617. PMID: 6254033, PMCID: PMC349895, DOI: 10.1073/pnas.77.8.4614.Peer-Reviewed Original ResearchConceptsT4 DNA replication proteinsDNA replication proteinsDNA-binding proteinsHelix-destabilizing proteinGene 32 proteinProtein-protein interactionsAmino acid sequenceLimited trypsin digestionProtein self-associationGene 32Replication proteinsUnusual stretchesSerine residuesCyanogen bromide cleavageDNA bindingAcid sequenceTyrosine residuesPrimary structureStaphylococcal proteasePartial proteolysisIntact proteinPosition 73Amino acidsTryptic peptidesProtein