1994
Purification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extracts.
Amrute S, Abdul-Manan Z, Pandey V, Williams K, Modak M. Purification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extracts. Biochemistry 1994, 33: 8282-91. PMID: 7518245, DOI: 10.1021/bi00193a015.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCattleCell NucleusChromatographyChromatography, High Pressure LiquidCross-Linking ReagentsCyanogen BromideDNA, Single-StrandedHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataOligodeoxyribonucleotidesPeptide FragmentsRibonucleoproteinsRNASpectrometry, FluorescenceThymus GlandUltraviolet RaysConceptsHnRNP proteinsOccluded site sizeHeterogeneous nuclear ribonucleoproteinsNucleic acidsSingle-strand nucleic acidNH2-terminal sequencingEukaryotic RNATight tetramerSDS-polyacrylamide gel electrophoresisApparent molecular weightNuclear ribonucleoproteinNuclear extractsLimited proteolysisMass spectrometric analysisRNAProteinPhenylalanine 19Calf thymusGel electrophoresisAdditional ionic interactionsTerminal deoxynucleotidyl transferaseSite sizeAB formMajor siteCell disruption
1986
Gene 32 protein, the single-stranded DNA binding protein from bacteriophage T4, is a zinc metalloprotein.
Giedroc D, Keating K, Williams K, Konigsberg W, Coleman J. Gene 32 protein, the single-stranded DNA binding protein from bacteriophage T4, is a zinc metalloprotein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 8452-8456. PMID: 3490667, PMCID: PMC386948, DOI: 10.1073/pnas.83.22.8452.Peer-Reviewed Original ResearchConceptsGene 32 proteinApo-g32PT4-infected Escherichia coliBacteriophage T4-infected Escherichia coliTyrosine-rich sequenceP-hydroxymercuriphenylsulfonatePlasmid pKC30Sequence CysBacteriophage T4Limited proteolysisConformational elementsEscherichia coliProteinDNAEDTA resultsG32PCysteineFragment ASide chainsPKC30ComplexesProteolysisColiSequenceLinear incorporationPurification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins.
Kumar A, Williams K, Szer W. Purification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins. Journal Of Biological Chemistry 1986, 261: 11266-11273. PMID: 3733753, DOI: 10.1016/s0021-9258(18)67378-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceChromatography, High Pressure LiquidCircular DichroismDNA-Binding ProteinsHeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsHumansMolecular WeightRibonucleoproteinsSpectrophotometry, UltravioletTrypsinConceptsHeterogeneous nuclear ribonucleoproteinsNucleic acid-binding domainProtein A1Glycine-rich proteinSsDNA-binding proteinDNA-binding proteinsHnRNP protein A1Helix-destabilizing activityHnRNP proteinsNuclear ribonucleoproteinTerminal domainHDP-1A1 bindsGlycine residueNative proteinPrimary structureLimited proteolysisHeLa cellsProtein A2Amino acidsProtein
1983
Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins.
Williams K, Spicer E, LoPresti M, Guggenheimer R, Chase J. Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins. Journal Of Biological Chemistry 1983, 258: 3346-3355. PMID: 6298232, DOI: 10.1016/s0021-9258(18)32867-9.Peer-Reviewed Original ResearchConceptsCOOH terminusBacteriophage T4 gene 32 proteinDNA-induced conformational changesT4 gene 32 proteinConformational changesEscherichia coliHelix-destabilizing proteinGene 32 proteinE. coli DNA replicationSimilar functional domainsCOOH-terminal domainLimited proteolysis studiesEukaryotic DNADNA replicationDouble-helical DNAHomologous domainsTerminal domainFunctional domainsT4 DNAProteolysis studiesLimited proteolysisTerminal regionAmino acidsProteinHelical DNA