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
1989
Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles
Merrill B, Barnett S, LeStourgeon W, Williams K. Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles. Nucleic Acids Research 1989, 17: 8441-8449. PMID: 2587210, PMCID: PMC335017, DOI: 10.1093/nar/17.21.8441.Peer-Reviewed Original ResearchConceptsInsert sequenceHeterogeneous nuclear ribonucleoprotein particleSingle transcription unitAlternative splicing mechanismNuclear ribonucleoprotein particleAmino acid sequencingResidue insertHnRNP proteinsTranscription unitTryptic peptide mappingSplicing mechanismPrimary structure differencesC2 proteinSDS-polyacrylamide gel electrophoresisNuclear ribonucleoproteinProtein C1Ribonucleoprotein particleUntranslated regionPrimary structurePolyacrylamide gel electrophoresisAmino acidsPeptide mappingGel electrophoresisMolecular weight differencesProtein
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 sitesPeptidesUse of HPLC Comparative Peptide Mapping in Structure/Function Studies
Williams K, Stone K, Fritz M, Merrill B, Konigsberg W, Pandolfo M, Valentini O, Riva S, Reddigari S, Patel G, Chase J. Use of HPLC Comparative Peptide Mapping in Structure/Function Studies. 1987, 45-52. DOI: 10.1007/978-1-4613-1787-6_5.Peer-Reviewed Original ResearchComparative peptide mappingPeptide mappingActive site peptideGroup-specific reagentsStructure/function studiesGas-phase sequencingProtein structureChemical modificationActive siteCovalent crosslinkingEnzymatic digestsReversed-phase HPLCSite peptideRetention timeSpecific reagentsPhase sequencingHPLCStructureBaseline artifactsIndividual amino acidsLigandsSpecific applicationsPeptidesReagentsAmino acids
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