Structure specific chromatographic selection in targeted proteomics

Hamid Mirzaei, Fred Regnier

Research output: Contribution to journalReview articlepeer-review

27 Scopus citations

Abstract

The whole proteome of any organism is too complicated to be analyzed in a simple one-step process and direct attempts for the entire proteome analysis normally lead to considerable loss of information. A practical approach is the targeting of the specific structural feature of interest using chromatography. This approach simplifies the proteome while preserving most of the vital information necessary for analysis. Selection of peptides with specific amino acids (cysteine, histidine and methionine) or N- or C-terminal peptides is an accepted procedure for proteome simplification when general analysis is desired. While selection of enzymatically and non-enzymatically modified proteins and peptides is used when post-translational modifications are targeted. Protein interaction with small molecules as well as other proteins also has been studied using chromatographic selection methods.

Original languageEnglish (US)
Pages (from-to)23-34
Number of pages12
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume817
Issue number1
DOIs
StatePublished - Mar 5 2005

Keywords

  • Affinity selection
  • Amino acid
  • Chromatography
  • Glycation
  • Glycosylation
  • Nitration
  • Oxidation
  • Phosphorylation
  • Proteomics
  • Specific amino acid selection

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry
  • Cell Biology

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