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, FungalRNA-Binding ProteinsSaccharomyces 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
1991
Single‐stranded DNA binding proteins (SSBs) from prokaryotic transmissible plasmids
Ruvolo P, Keating K, Williams K, Chase J. Single‐stranded DNA binding proteins (SSBs) from prokaryotic transmissible plasmids. Proteins Structure Function And Bioinformatics 1991, 9: 120-134. PMID: 2008432, DOI: 10.1002/prot.340090206.Peer-Reviewed Original ResearchConceptsAmino acid residuesSSB proteinDNA bindingE. coli SSB proteinAcid residuesHelix-destabilizing proteinsEscherichia coli SSBAmino acid sequenceNH2-terminal regionCOOH-terminal regionProteins divergeSequence comparisonProtein sequencesSequence homologyAcid sequenceF plasmidPhe-60Trp-40Trp-54NH2-terminalTerminal thirdDNA binding studiesElongation rateTyr-70Protein
1990
Purification and functional characterization of adenovirus ts111A DNA-binding protein. Fluorescence studies of protein-nucleic acid binding.
Meyers M, Keating K, Roberts W, Williams K, Chase J, Horwitz M. Purification and functional characterization of adenovirus ts111A DNA-binding protein. Fluorescence studies of protein-nucleic acid binding. Journal Of Biological Chemistry 1990, 265: 5875-5882. PMID: 2318838, DOI: 10.1016/s0021-9258(19)39444-x.Peer-Reviewed Original Research
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