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An improved model for prediction of retention times of tryptic peptides in ion pair reversed-phase HPLC: its application to protein peptide mapping by off-line HPLC-MALDI MS.
Krokhin, O V; Craig, R; Spicer, V; Ens, W; Standing, K G; Beavis, R C; Wilkins, J A.
Afiliación
  • Krokhin OV; Department of Physics and Astronomy, University of Manitoba, Winnipeg, MB, R3T 2N2, Canada. krokhino@cc.umanitoba.ca
Mol Cell Proteomics ; 3(9): 908-19, 2004 Sep.
Article en En | MEDLINE | ID: mdl-15238601
The proposed model is based on the measurement of the retention times of 346 tryptic peptides in the 560- to 4,000-Da mass range, derived from a mixture of 17 protein digests. These peptides were measured in HPLC-MALDI MS runs, with peptide identities confirmed by MS/MS. The model relies on summation of the retention coefficients of the individual amino acids, as in previous approaches, but additional terms are introduced that depend on the retention coefficients for amino acids at the N-terminal of the peptide. In the 17-protein mixture, optimization of two sets of coefficients, along with additional compensation for peptide length and hydrophobicity, yielded a linear dependence of retention time on hydrophobicity, with an R2 value about 0.94. The predictive capability of the model was used to distinguish peptides with close m/z values and for detailed peptide mapping of selected proteins. Its applicability was tested on columns of different sizes, from nano- to narrow-bore, and for direct sample injection, or injection via a pre-column. It can be used for accurate prediction of retention times for tryptic peptides on reversed-phase (300-A pore size) columns of different sizes with a linear water-ACN gradient and with TFA as the ion-pairing modifier.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fragmentos de Péptidos / Mapeo Peptídico / Cromatografía Líquida de Alta Presión / Espectrometría de Masa por Láser de Matriz Asistida de Ionización Desorción Tipo de estudio: Prognostic_studies / Risk_factors_studies Límite: Animals / Humans Idioma: En Revista: Mol Cell Proteomics Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2004 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fragmentos de Péptidos / Mapeo Peptídico / Cromatografía Líquida de Alta Presión / Espectrometría de Masa por Láser de Matriz Asistida de Ionización Desorción Tipo de estudio: Prognostic_studies / Risk_factors_studies Límite: Animals / Humans Idioma: En Revista: Mol Cell Proteomics Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2004 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos