title: Structure specific chromatographic selection in targeted proteomics.
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.
authors.affiliation: Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN 47907-2084, USA.
authors.forename: Hamid
authors.initials: H
authors.lastname: Mirzaei
authors.forename: Fred
authors.initials: F
authors.lastname: Regnier
mesh_terms: D002845:Chromatography / Q000379:methods*; D010455:Peptides / Q000737:chemistry; D011506:Proteins / Q000737:chemistry; D040901:Proteomics
chemical_list: D010455:Peptides; D011506:Proteins