2024
Optimal conditions for carrying out trypsin digestions on complex proteomes: From bulk samples to single cells
Mansuri M, Bathla S, Lam T, Nairn A, Williams K. Optimal conditions for carrying out trypsin digestions on complex proteomes: From bulk samples to single cells. Journal Of Proteomics 2024, 297: 105109. PMID: 38325732, PMCID: PMC10939724, DOI: 10.1016/j.jprot.2024.105109.Peer-Reviewed Original ResearchComplex proteomesProtein cleavage activityOptimal conditionsTrypsin digestion protocolReversed phase HPLC separationMass spectrometry workflowMS-based proteomicsMass spectrometric analysisC-terminal amino acid residuesTrypsin digestionChromatographic separationDigestion protocolAmino acid residuesHPLC separationMS/MS analysisGlobal proteomic analysisSingle cellsSample matrixSpectrometric analysisCleavage specificityGeneration of peptidesAcid residuesDown proteinsProteomic analysisCleavage activity
2009
Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels
Stone K, Gulcicek E, Williams K. Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels. Springer Protocols Handbooks 2009, 905-917. DOI: 10.1007/978-1-59745-198-7_99.Peer-Reviewed Original ResearchProtein of interestSDS-polyacrylamide gelsMass spectrometryGel digestion procedureChemical sequencingLaser desorption ionization mass spectrometryDesorption ionization mass spectrometryElectrospray ionization sourceIonization mass spectrometryComplex biological mixturesMass spectral acquisitionProtein identification analysisTandem mass spectrometrySDS-PAGEMass spectrometric analysisPolyacrylamide gelsIonization sourceNumerous genomesBiological mixturesPeptide mass dataProtein databaseCleavage procedureMass spectrometerGel matrixLC system
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