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Neutron-encoded signatures enable product ion annotation from tandem mass spectra.
Richards, Alicia L; Vincent, Catherine E; Guthals, Adrian; Rose, Christopher M; Westphall, Michael S; Bandeira, Nuno; Coon, Joshua J.
Afiliación
  • Richards AL; Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706;
Mol Cell Proteomics ; 12(12): 3812-23, 2013 Dec.
Article en En | MEDLINE | ID: mdl-24043425
We report the use of neutron-encoded (NeuCode) stable isotope labeling of amino acids in cell culture for the purpose of C-terminal product ion annotation. Two NeuCode labeling isotopologues of lysine, (13)C6(15)N2 and (2)H8, which differ by 36 mDa, were metabolically embedded in a sample proteome, and the resultant labeled proteins were combined, digested, and analyzed via liquid chromatography and mass spectrometry. With MS/MS scan resolving powers of ~50,000 or higher, product ions containing the C terminus (i.e. lysine) appear as a doublet spaced by exactly 36 mDa, whereas N-terminal fragments exist as a single m/z peak. Through theory and experiment, we demonstrate that over 90% of all y-type product ions have detectable doublets. We report on an algorithm that can extract these neutron signatures with high sensitivity and specificity. In other words, of 15,503 y-type product ion peaks, the y-type ion identification algorithm correctly identified 14,552 (93.2%) based on detection of the NeuCode doublet; 6.8% were misclassified (i.e. other ion types that were assigned as y-type products). Searching NeuCode labeled yeast with PepNovo(+) resulted in a 34% increase in correct de novo identifications relative to searching through MS/MS only. We use this tool to simplify spectra prior to database searching, to sort unmatched tandem mass spectra for spectral richness, for correlation of co-fragmented ions to their parent precursor, and for de novo sequence identification.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Algoritmos / Proteoma / Proteínas de Saccharomyces cerevisiae / Anotación de Secuencia Molecular / Marcaje Isotópico / Neutrones Idioma: En Revista: Mol Cell Proteomics Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2013 Tipo del documento: Article Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Algoritmos / Proteoma / Proteínas de Saccharomyces cerevisiae / Anotación de Secuencia Molecular / Marcaje Isotópico / Neutrones Idioma: En Revista: Mol Cell Proteomics Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2013 Tipo del documento: Article Pais de publicación: Estados Unidos