This article is part of the supplement: Proceedings of the 2007 and 2008 Symposia on Protein N-terminal Acetylation

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A review of COFRADIC techniques targeting protein N-terminal acetylation

Petra Van Damme1,2, Jozef Van Damme1,2, Hans Demol1,2, An Staes1,2, Joël Vandekerckhove1,2 and Kris Gevaert1,2*

Author Affiliations

1 Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium

2 Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium

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BMC Proceedings 2009, 3(Suppl 6):S6 doi:10.1186/1753-6561-3-S6-S6

Published: 4 August 2009

Abstract

Acetylation of nascent protein Nα-termini is a common modification among archae and eukaryotes and can influence the structure and function of target proteins. This modification has been studied on an individual protein or (synthetic) peptide level or on a proteome scale using two-dimensional polyacrylamide gel electrophoresis. We recently developed mass spectrometry driven proteome analytical approaches specifically targeting the amino (N) terminus of proteins based on the concept of diagonal reverse-phase chromatography. We here review how this so-called combined fractional diagonal chromatography (COFRADIC) technique can be used in combination with differential mass-tagging strategies as to both qualitatively and quantitatively assess protein Nα-acetylation in whole proteomes.