1990
[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
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
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
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
1977
Purification and some properties of Escherichia coli tRNA nucleotidyltransferase.
Schofield P, Williams K. Purification and some properties of Escherichia coli tRNA nucleotidyltransferase. Journal Of Biological Chemistry 1977, 252: 5584-5588. PMID: 328503, DOI: 10.1016/s0021-9258(19)63390-9.Peer-Reviewed Original ResearchConceptsTransition metal chelating agentsMetal chelating agentsSodium dodecyl sulfate gel electrophoresisDodecyl sulfate gel electrophoresisSulfate gel electrophoresisTurnover numberChelating agentOverall yieldMolecular weightPure enzymeIsoelectric pointKey stepIdentical isoelectric pointsSephadex chromatographyCrude extractPurificationAffinity columnGel electrophoresisEscherichia coli tRNA nucleotidyltransferaseSpecific activityAssay conditionsChromatographyEnzymeTRNA nucleotidyltransferaseOptimal assay conditions