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Titolo:
SEQUENCE TAG IDENTIFICATION OF INTACT PROTEINS BY MATCHING TANDEM MASS-SPECTRAL DATA AGAINST SEQUENCE DATA-BASES
Autore:
MORTZ E; OCONNOR PB; ROEPSTORFF P; KELLEHER NL; WOOD TD; MCLAFFERTY FW; MANN M;
Indirizzi:
ODENSE UNIV,DEPT MOL BIOL,CAMPUSVEJ 55 DK-5230 ODENSE M DENMARK EUROPEAN MOL BIOL LAB D-69012 HEIDELBERG GERMANY CORNELL UNIV,BAKER LAB,DEPT CHEM ITHACA NY 14853
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 16, volume: 93, anno: 1996,
pagine: 8264 - 8267
SICI:
0027-8424(1996)93:16<8264:STIOIP>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
MULTIPLY-CHARGED IONS; INFRARED MULTIPHOTON DISSOCIATION; ELECTROSPRAY IONIZATION; SPECTROMETRIC PEPTIDE; GENOME PROJECT; DATABASES; INFORMATION; GELS;
Keywords:
PROTEIN SEQUENCING; PROTEIN MODIFICATION; ELECTROSPRAY MASS SPECTROMETRY; DATA BASE SEARCH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
E. Mortz et al., "SEQUENCE TAG IDENTIFICATION OF INTACT PROTEINS BY MATCHING TANDEM MASS-SPECTRAL DATA AGAINST SEQUENCE DATA-BASES", Proceedings of the National Academy of Sciences of the United Statesof America, 93(16), 1996, pp. 8264-8267

Abstract

Molecular and fragment ion data of intact 8- to 43-kDa proteins from electrospray Fourier-transform tandem mass spectrometry are matched against the corresponding data in sequence data bases. Extending the sequence tag concept of Mann and Wilm for matching peptides, a partial amino acid sequence in the unknown is first identified from the mass differences of a series of fragment ions, and the mass position of this sequence is defined from molecular weight and the fragment ion masses, For three studied proteins, a single sequence tag retrieved only the correct protein from the data base; a fourth protein required the inputof two sequence tags. However, three of the data base proteins differed by having an extra methionine or by missing an acetyl or heme substitution. The positions of these modifications in the protein examined were greatly restricted by the mass differences of its molecular and fragment ions versus those of the data base, To characterize the primary structure of an unknown represented in the data base, this method isfast and specific and does not require prior enzymatic or chemical degradation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 00:18:06