1997
Enzymatic cleavage and HPLC peptide mapping of proteins
Williams K, Stone K. Enzymatic cleavage and HPLC peptide mapping of proteins. Molecular Biotechnology 1997, 8: 155-167. PMID: 9406186, DOI: 10.1007/bf02752260.Peer-Reviewed Original Research
1995
Identifying Sites of Posttranslational Modifications in Proteins Via HPLC Peptide Mapping
Williams K, Stone K. Identifying Sites of Posttranslational Modifications in Proteins Via HPLC Peptide Mapping. Methods In Molecular Biology 1995, 40: 157-175. PMID: 7633521, DOI: 10.1385/0-89603-301-5:157.Peer-Reviewed Original ResearchConceptsHPLC peptide mappingMass spectrometryPosttranslational modificationsIntact proteinPeptide mappingAtomic mass unitsAccurate massNet chargeDifferent posttranslational modificationsSulfoxide formationMass unitsCovalent changesOxidationSpectrometryProtein stabilityDeamidationProteinIsoelectric focusingPhosphorylationModification
1992
Purification 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 SpecificityUltracentrifugation
1988
Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids.
Cobianchi F, Karpel R, Williams K, Notario V, Wilson S. Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids. Journal Of Biological Chemistry 1988, 263: 1063-1071. PMID: 2447078, DOI: 10.1016/s0021-9258(19)35461-4.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsBase SequenceCelluloseDNADNA, Single-StrandedEscherichia coliFluorescent DyesHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataPoly ARecombinant ProteinsRibonucleoproteinsRNAConceptsLarge-scale overproductionNH2-terminal domainTerminal domainDomain peptideCooperative protein-protein interactionsEscherichia coliProtein-induced fluorescence enhancementAmino acidsProtein-protein interactionsNucleic acidsAlpha-helix structureProtein A1Cooperative bindingAssociation constantsSynthetic polypeptide analogueProteinDirect interactionNatural proteinsRecombinant A1Low association constantsBindingIntact A1ColiFluorescence enhancementOverproductionSynthesis of the p10 single-stranded nucleic acid binding protein from murine leukemia virus.
Roberts W, Elliott J, McMurray W, Williams K. Synthesis of the p10 single-stranded nucleic acid binding protein from murine leukemia virus. Chemical Biology & Drug Design 1988, 1: 74-80. PMID: 2856555.Peer-Reviewed Original ResearchConceptsBeta strandsAlpha-helixDirect amino acid sequencingSynthetic peptide bindsMurine leukemia virus proteinsAmino acid sequencingLys-C peptidesRetroviral Gag polyproteinFasman analysisGene 32Nucleic acidsP10 proteinCircular dichroism experimentsCys-X2Cysteine positionsBacteriophage T4Endoproteinase Lys-C peptidesPrimary sequenceMurine leukemia virusNative proteinPrimary structureCys-X4Amino acid analysisProteinSimilar sequences
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
1986
High-performance liquid chromatographic peptide mapping and amino acid analysis in the sub-nanomole range
Stone K, Williams K. High-performance liquid chromatographic peptide mapping and amino acid analysis in the sub-nanomole range. Journal Of Chromatography 1986, 359: 203-212. PMID: 3733927, DOI: 10.1016/0021-9673(86)80074-7.Peer-Reviewed Original ResearchHigh pressure liquid chromatography purification of UP1 and UP2, two related single-stranded nucleic acid-binding proteins from calf thymus.
Merrill B, LoPresti M, Stone K, Williams K. High pressure liquid chromatography purification of UP1 and UP2, two related single-stranded nucleic acid-binding proteins from calf thymus. Journal Of Biological Chemistry 1986, 261: 878-883. PMID: 3941105, DOI: 10.1016/s0021-9258(17)36178-1.Peer-Reviewed Original Research
1984
Photochemical cross-linking of the Escherichia coli single-stranded DNA-binding protein to oligodeoxynucleotides. Identification of phenylalanine 60 as the site of cross-linking.
Merrill B, Williams K, Chase J, Konigsberg W. Photochemical cross-linking of the Escherichia coli single-stranded DNA-binding protein to oligodeoxynucleotides. Identification of phenylalanine 60 as the site of cross-linking. Journal Of Biological Chemistry 1984, 259: 10850-10856. PMID: 6540775, DOI: 10.1016/s0021-9258(18)90591-0.Peer-Reviewed Original ResearchConceptsReversed-phase ion-pair high-performance liquid chromatographyIon-pair high-performance liquid chromatographySolid-phase sequence analysisFuture structure/function studiesPeptide-oligonucleotide complexesHigh-performance liquid chromatographyProtein-oligonucleotide complexesLiquid chromatographyPurification procedurePeptide complexesUltraviolet irradiationComplexesStructure/function studiesUltraviolet lightPeptide comprisingCalf thymusGeneral applicabilityAmino acidsChromatographyNucleic acid-binding proteinsReactionThymineExtensive studyIrradiationAcid
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
1979
Structural characteristics of interferons from mouse Ehrlich ascites tumor cells.
Cabrer B, Taira H, Broeze R, Kempe T, Williams K, Slattery E, Konigsberg W, Lengyel P. Structural characteristics of interferons from mouse Ehrlich ascites tumor cells. Journal Of Biological Chemistry 1979, 254: 3681-3684. PMID: 438151, DOI: 10.1016/s0021-9258(18)50635-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsAnimalsCarcinoma, Ehrlich TumorInterferonsMiceMolecular WeightPeptide FragmentsTrypsinConceptsAmino acidsMouse EhrlichNH2-terminal amino acidsTryptic peptide mapsSmaller speciesLarger speciesPeptide mapsSpeciesTumor cellsSize classesNewcastle disease virusDisease virusSpecific activityCellsGlycosylationProteinUnits/AcidEhrlichCarboxypeptidaseInterferonIsolationStructural characteristics
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 ResearchConceptsGene 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