Journal
FEBS JOURNAL
Volume 274, Issue 24, Pages 6277-6289Publisher
WILEY
DOI: 10.1111/j.1742-4658.2007.06149.x
Keywords
activity-based probe; ATP-binding proteins; COFRADIC; diagonal chromatography; N-terminal peptides; peptide sorting; protein N-glycosylation; protein processing
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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 were profiled by diagonal chromatography.
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