Technical Brief

Sweet Substitute: A software tool for in silico fragmentation of peptide-linked N-glycans

  1. Stefan Clerens1,*,
  2. Wim Van den Ende2,
  3. Peter Verhaert3,
  4. Lieve Geenen1,
  5. Lutgarde Arckens1

Article first published online: 17 SEP 2003

DOI: 10.1002/pmic.200300572

Issue

PROTEOMICS

PROTEOMICS

Volume 4, Issue 3, pages 629–632, March 2004

Additional Information

How to Cite

Clerens, S., Van den Ende, W., Verhaert, P., Geenen, L. and Arckens, L. (2004), Sweet Substitute: A software tool for in silico fragmentation of peptide-linked N-glycans. PROTEOMICS, 4: 629–632. doi: 10.1002/pmic.200300572

Author Information

  1. 1

    Laboratory of Neuroplasticity and Neuroproteomics, K. U. Leuven, Leuven, Belgium

  2. 2

    Laboratory of Developmental Biology, K. U. Leuven, Heverlee, Belgium

  3. 3

    Organon NV, Proteomics Group, Target Discovery Unit, Oss, The Netherlands

*Laboratory of Neuroplasticity and Neuroproteomics, K. U. Leuven, Naamsestraat 59, B-3000 Leuven, Belgium Fax: +32-16-32-4263

Publication History

  1. Issue published online: 19 FEB 2004
  2. Article first published online: 17 SEP 2003
  3. Manuscript Received: 6 MAY 2003

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Keywords:

  • Glycosylation;
  • Mass spectrometry;
  • N-linked glycane;
  • Tandem mass spectrometry

Abstract

A software tool, Sweet Substitute, is described, which assists tandem mass spectrometry (MS/MS)-based glycosylation characterization from within a tryptic digest. The algorithm creates a virtual nanoelectrospray-quadrupole time-of-flight style-MS/MS spectrum of any user-defined N-linked glycan structure. An empirical peak height modeling routine is implemented in the program. By comparing the theoretical MS/MS data with the deconvoluted and deisotoped experimental MS/MS data, the user is able to quickly assess whether a proposed candidate oligosaccharide structure is a plausible one.

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