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Titolo:
Informatics and multiplexing of intact protein identification in bacteria and the archaea
Autore:
Meng, FY; Cargile, BJ; Miller, LM; Forbes, AJ; Johnson, JR; Kelleher, NL;
Indirizzi:
Univ Illinois, Dept Chem, Urbana, IL 61801 USA Univ Illinois Urbana IL USA 61801 linois, Dept Chem, Urbana, IL 61801 USA
Titolo Testata:
NATURE BIOTECHNOLOGY
fascicolo: 10, volume: 19, anno: 2001,
pagine: 952 - 957
SICI:
1087-0156(200110)19:10<952:IAMOIP>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
INFRARED MULTIPHOTON DISSOCIATION; RESONANCE MASS-SPECTROMETRY; ELECTRON-CAPTURE DISSOCIATION; SEQUENCE DATABASES; ESCHERICHIA-COLI; METHANOCOCCUS-JANNASCHII; PHOSPHORYLATION; PEPTIDES; MIXTURES; IONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Kelleher, NL Univ Illinois, Dept Chem, 1209 W Calif St, Urbana, IL 61801 USA Univ Illinois 1209 W Calif St Urbana IL USA 61801 L 61801 USA
Citazione:
F.Y. Meng et al., "Informatics and multiplexing of intact protein identification in bacteria and the archaea", NAT BIOTECH, 19(10), 2001, pp. 952-957

Abstract

Although direct fragmentation of protein ions in a mass spectrometer is far more efficient than exhaustive mapping of 1-3 kDa peptides for complete characterization of primary structures predicted from sequenced genomes, thedevelopment of this approach is still in its infancy. Here we describe a statistical model (good to within similar to5%) that shows that the databasesearch specificity of this method requires only three of four fragment ions to match (at +/-0.1 Da) for a 99.8% probability of being correct in a database of 5,000 protein forms. Software developed for automated processing of protein ion fragmentation data and for probability-based retrieval of whole proteins is illustrated by identification of 18 archaeal and bacterial proteins with simultaneous mass-spectro metric (MS) mapping of their entire primary structures. Dissociation of two or three proteins at once for such identifications in parallel is also demonstrated, along with retention and exact localization of a phosphorylated serine residue through the fragmentation process. These conceptual and technical advances should assist future processing of whole proteins in a higher throughput format for more robust detection of co- and post-translational modifications.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 19:51:54