Improving de Novo Sequencing of Peptides Using a Charged Tag and C-Terminal Digestion

peer-reviewed · Analytical Chemistry · 2007

peer-reviewed · Analytical Chemistry · 2007. Weibin Chen et al. An improved method for peptide de novo sequencing by MALDI mass spectrometry is presented. The method couples…
Date 2007-02-01
Type peer-reviewed
Venue Analytical Chemistry
Publisher American Chemical Society (ACS)
Contribution algorithm
DOI 10.1021/ac061670b
Citations (OpenAlex) 48
Venue 2-year citedness 7.10

Abstract

An improved method for peptide de novo sequencing by MALDI mass spectrometry is presented. The method couples a charge derivatization reaction with C-terminal digestion to modify tryptic peptides. The charge derivatization attaches a fixed charge group onto the N-termini of peptides, and the enzymatic digestion after the derivatization step removes C-terminal basic amino acid residues such as arginine and lysine. The fragmentation of the modified peptide(s) under low-energy CID conditions (MALDI Q-TOF mass spectrometer) yields a simplified yet complete ion series of the peptide sequence. The validity of the method is demonstrated by the results from several model protein digests, where peptide sequences were correctly deduced either manually or through an automated sequencing program.

Authors

  1. Weibin Chen
  2. Peter J. Lee
  3. Henry Shion
  4. Nicholas Ellor
  5. John C. Gebler

Methods and tools

  • Charged tag with C-terminal digestion: Couples a fixed-charge N-terminal derivatization with a C-terminal digestion of the derivatized peptide, so MALDI spectra carry one interpretable series and the ladder can be read directly.

Cites (1)

Cited by (4)

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