1992
Shuffling of amino acid sequence: an important control in synthetic peptide studies of nucleic acid-binding domains. Binding properties of fragments of a conserved eukaryotic RNA binding motif.
Nadler S, Kapouch J, Elliott J, Williams K. Shuffling of amino acid sequence: an important control in synthetic peptide studies of nucleic acid-binding domains. Binding properties of fragments of a conserved eukaryotic RNA binding motif. Journal Of Biological Chemistry 1992, 267: 3750-3757. PMID: 1740426, DOI: 10.1016/s0021-9258(19)50589-0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCarrier ProteinsCircular DichroismFungal ProteinsGenes, FungalHot TemperatureMolecular Sequence DataNucleic Acid DenaturationNucleic AcidsPeptide FragmentsPoly APoly A-UPoly(A)-Binding ProteinsRNA-Binding ProteinsRNA, FungalSaccharomyces cerevisiaeSpectrometry, FluorescenceSubstrate SpecificityConceptsNucleic acidsPeptide studiesResidue peptideSynthetic peptide studiesSynthetic peptidesSynthetic peptide analoguesFree energyProperties of fragmentsPeptide analoguesNucleic acid-binding domainParent proteinLatter peptideNucleic acid bindingAmino acidsStructure/function studiesAmino acid sequenceSignificant affinityAcidEukaryotic RNAPeptidesRNA specificityAmino acid compositionSimilar RNACarboxyl halfMolecular basis
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
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