TAILIEUCHUNG - Báo cáo khoa học: Applications of diagonal chromatography for proteomewide characterization of protein modifications and activity-based analyses

Numerous gel-free proteomics techniques have been reported over the past few years, introducing a move from proteins to peptides as bits of informa-tion in qualitative and quantitative proteome studies. Many shotgun pro-teomics techniques randomly sample thousands of peptides in a qualitative and quantitative manner but overlook the vast majority of protein modifi-cations that are often crucial for proper protein structure and function. | ỊFEBS Journal MINIREVIEW Applications of diagonal chromatography for proteome-wide characterization of protein modifications and activity-based analyses Kris Gevaert1 2 Francis Impens1 2 Petra Van Damme1 2 Bart Ghesquiere1 2 Xavier Hanoulle3 and Joel Vandekerckhove1 2 1 Department of MedicalProtein Research VIB Ghent Belgium 2 Department of Biochemistry Ghent University Belgium 3 UMR 8576 CNRS - University of Sciences and Technologies of Lille Structuraland FunctionalGlycobiology Unit Villeneuve d Ascq France Keywords activity-based probe ATP-binding proteins COFRADIC diagonal chromatography N-terminalpeptides peptide sorting protein N-glycosylation protein processing Correspondence K. Gevaert Department of Biochemistry Faculty of Medicine and Health Sciences Ghent University A. Baertsoenkaai 3 B-9000 Ghent Belgium Fax 32 92649496 Tel 32 92649274 E-mail Website http Received 24 April2007 revised 10 September 2007 accepted 17 October 2007 Numerous gel-free proteomics techniques have been reported over the past few years introducing a move from proteins to peptides as bits of information in qualitative and quantitative proteome studies. Many shotgun proteomics techniques randomly sample thousands of peptides in a qualitative and quantitative manner but overlook the vast majority of protein modifications that are often crucial for proper protein structure and function. Peptide-based proteomic approaches have thus been developed to profile a diverse set of modifications including but not at all limited to phosphorylation glycosylation and ubiquitination. Typical here is that each modification needs a specific tailor-made analytical procedure. In this minireview we discuss how one technique - diagonal reverse-phase chromatography - is applied to study two different types of protein modification protein processing and protein N-glycosylation. Additionally we discuss an activity-based proteome study in which purine-binding proteins

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