2002
Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins
Stone K, Williams K. Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins. 2002, 0: 533-540. DOI: 10.1385/1-59259-169-8:533.Peer-Reviewed Original ResearchReversed-phase HPLCEnzymatic digestsLaser desorption mass spectrometrySites of chemicalMatrix-assisted laser desorption mass spectrometryRelative elution positionsDesorption mass spectrometryMobile phase resultsReversed-phase HPLC separationTotal hydrophobicityAqueous mixturesMass spectrometryVolatile solventsReversephase HPLCHPLC separationLarge peptidesParticular separationComplex mixturesExcellent reproducibilitySlow kineticsEdman sequencingRetention coefficientTight bindingHydrophobic amino acidsHPLC
1996
Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins
Stone K, Williams K. Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins. Springer Protocols Handbooks 1996, 427-434. DOI: 10.1007/978-1-60327-259-9_72.Peer-Reviewed Original ResearchReversed-phase HPLCEnzymatic digestsLaser desorption mass spectrometrySites of chemicalMatrix-assisted laser desorption mass spectrometryRelative elution positionsDesorption mass spectrometryMobile phase resultsReversed-phase HPLC separationTotal hydrophobicityAqueous mixturesMass spectrometryVolatile solventsHPLC separationLarge peptidesComplex mixturesParticular separationExcellent reproducibilitySlow kineticsEdman sequencingRetention coefficientTight bindingHydrophobic amino acidsHPLCRelative insolubility
1991
State‐of‐the‐art biomolecular core facilities: a comprehensive survey1
Niece R, Beach C, Cook R, Hathaway G, Williams K. State‐of‐the‐art biomolecular core facilities: a comprehensive survey1. The FASEB Journal 1991, 5: 2756-2760. PMID: 1916100, DOI: 10.1096/fasebj.5.13.1916100.Peer-Reviewed Original Research
1987
Use 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