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Titolo:
Protein identification with a single accurate mass of a cysteine-containing peptide and constrained database searching
Autore:
Goodlett, DR; Bruce, JE; Anderson, GA; Rist, B; Pasa-Tolic, L; Fiehn, O; Smith, RD; Aebersold, R;
Indirizzi:
Univ Washington, Dept Mol Biotechnol, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 ol Biotechnol, Seattle, WA 98195 USA Pacific NW Natl Lab, Environm Mol Sci Lab, Richland, WA 99352 USA Pacific NW Natl Lab Richland WA USA 99352 Sci Lab, Richland, WA 99352 USA Max Planck Inst Mol Plant Physiol, Potsdam, Germany Max Planck Inst Mol Plant Physiol Potsdam Germany iol, Potsdam, Germany Merck Res Labs, W Point, PA 19486 USA Merck Res Labs W Point PA USA 19486Merck Res Labs, W Point, PA 19486 USA
Titolo Testata:
ANALYTICAL CHEMISTRY
fascicolo: 6, volume: 72, anno: 2000,
pagine: 1112 - 1118
SICI:
0003-2700(20000315)72:6<1112:PIWASA>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
SEQUENCE DATABASES; SPECTROMETRY; ELECTROPHORESIS; GELS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Goodlett, DR Univ Washington, Dept Mol Biotechnol, Hlth Sci Bldg K327,Box 357730, Seattle, WA 98195 USA Univ Washington Hlth Sci Bldg K327,Box 357730Seattle WA USA 98195
Citazione:
D.R. Goodlett et al., "Protein identification with a single accurate mass of a cysteine-containing peptide and constrained database searching", ANALYT CHEM, 72(6), 2000, pp. 1112-1118

Abstract

A method for rapid and unambiguous identification of proteins by sequence database searching using the accurate mass of a single peptide and specificsequence constraints is described. Peptide masses were measured using electrospray ionization-Fourier transform ion cyclotron resonance mass spectrometry to an accuracy of 1 ppm. The presence of a cysteine residue within a peptide sequence was used as a database searching constraint to reduce the number of potential database hits. Cysteine-containing peptides were detected within a mixture of peptides by incorporating chlorine into a general alkylating reagent specific for cysteine residues. Secondary search constraints included the specificity of the protease used for protein digestion and the molecular mass of the protein estimated by gel electrophoresis. The natural isotopic distribution of chlorine encoded the cysteine-containing peptide with a distinctive isotopic pattern that allowed automatic screening of mass spectra. The method is demonstrated for a peptide standard and unknownproteins from a yeast lysate using all 6118 possible yeast open reading frames as a database. As judged by calculation of codon bias, low-abundance proteins were identified from the yeast lysate using this new method but notby traditional methods such as tandem mass spectrometry via data-dependentacquisition or mass mapping.

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Documento generato il 03/07/20 alle ore 21:35:21