{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Carabetta VJ"],"funding":["NIDA NIH HHS","NIGMS NIH HHS"],"pagination":["1050-60"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2873099"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["21(6)"],"pubmed_abstract":["The study of isolated protein complexes has greatly benefited from recent advances in mass spectrometry instrumentation and quantitative, isotope labeling techniques. The comprehensive characterization of protein complex components and quantification of their relative abundance relies heavily upon maximizing protein and peptide sequence information obtained from MS and tandem MS studies. Recent work has shown that using a metalloendopeptidase, Lys-N, for proteomic analysis of biological protein mixtures produces complementary protein sequence information compared with trypsin digestion alone. Here, we have investigated the suitability of Lys-N proteolysis for use with MALDI mass spectrometry to characterize the yeast Arp2 complex and E. coli PAP I protein interactions. Although Lys-N diges"],"journal":["Journal of the American Society for Mass Spectrometry"],"pubmed_title":["Integrating Lys-N proteolysis and N-terminal guanidination for improved fragmentation and relative quantification of singly-charged ions."],"pmcid":["PMC2873099"],"funding_grant_id":["GM65216","DP1 DA026192","R01 GM065216","DP1DA026192","DP1 DA026192-02","DP1 DA026192-01"],"pubmed_authors":["Carabetta VJ","Shakya A","Li T","Cristea IM","Greco TM"],"additional_accession":[]},"is_claimable":false,"name":"Integrating Lys-N proteolysis and N-terminal guanidination for improved fragmentation and relative quantification of singly-charged ions.","description":"The study of isolated protein complexes has greatly benefited from recent advances in mass spectrometry instrumentation and quantitative, isotope labeling techniques. The comprehensive characterization of protein complex components and quantification of their relative abundance relies heavily upon maximizing protein and peptide sequence information obtained from MS and tandem MS studies. Recent work has shown that using a metalloendopeptidase, Lys-N, for proteomic analysis of biological protein mixtures produces complementary protein sequence information compared with trypsin digestion alone. Here, we have investigated the suitability of Lys-N proteolysis for use with MALDI mass spectrometry to characterize the yeast Arp2 complex and E. coli PAP I protein interactions. Although Lys-N diges","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Jun","modification":"2025-04-26T00:46:52.747Z","creation":"2019-03-27T00:30:54Z"},"accession":"S-EPMC2873099","cross_references":{"pubmed":["20207164"],"doi":["10.1016/j.jasms.2010.02.004"]}}