In:
BMC Proceedings, Springer Science and Business Media LLC, Vol. 3, No. S6 ( 2009-12)
Abstract:
Acetylation of nascent protein N α -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 N α -acetylation in whole proteomes.
Type of Medium:
Online Resource
ISSN:
1753-6561
DOI:
10.1186/1753-6561-3-S6-S6
Language:
English
Publisher:
Springer Science and Business Media LLC
Publication Date:
2009
detail.hit.zdb_id:
2411867-9
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