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BioMed Central, BMC Proceedings, S6(3), 2009

DOI: 10.1186/1753-6561-3-s6-s6

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A review of COFRADIC techniques targeting protein N-terminal acetylation

Journal article published in 2009 by Petra Van Damme ORCID, Jozef Van Damme, Hans Demol, An Staes, Joël Vandekerckhove, Kris Gevaert ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.