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A review of COFRADIC techniques targeting protein N-terminal acetylation

Petra Van Damme (UGent), Jozef Van Damme (UGent), Hans Demol (UGent), An Staes (UGent), Joël Vandekerckhove (UGent) and Kris Gevaert (UGent)
(2009) BMC PROCEEDINGS. 3(suppl. 6).
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Abstract
Acetylation of nascent protein Nalpha-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 Nalpha-acetylation in whole proteomes.

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Chicago
Van Damme, Petra, Jozef Van Damme, Hans Demol, An Staes, Joël Vandekerckhove, and Kris Gevaert. 2009. “A Review of COFRADIC Techniques Targeting Protein N-terminal Acetylation.” In Bmc Proceedings. Vol. 3.
APA
Van Damme, Petra, Van Damme, J., Demol, H., Staes, A., Vandekerckhove, J., & Gevaert, K. (2009). A review of COFRADIC techniques targeting protein N-terminal acetylation. BMC PROCEEDINGS (Vol. 3). Presented at the NAT 2007 and 2008 Symposia : Protein N-terminal acetylation and protein N-terminal acetyltransferases (NATs).
Vancouver
1.
Van Damme P, Van Damme J, Demol H, Staes A, Vandekerckhove J, Gevaert K. A review of COFRADIC techniques targeting protein N-terminal acetylation. BMC PROCEEDINGS. 2009.
MLA
Van Damme, Petra, Jozef Van Damme, Hans Demol, et al. “A Review of COFRADIC Techniques Targeting Protein N-terminal Acetylation.” Bmc Proceedings. Vol. 3. 2009. Print.
@inproceedings{725501,
  abstract     = {Acetylation of nascent protein Nalpha-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 Nalpha-acetylation in whole proteomes.},
  articleno    = {S6},
  author       = {Van Damme, Petra and Van Damme, Jozef and Demol, Hans and Staes, An and Vandekerckhove, Jo{\"e}l and Gevaert, Kris},
  booktitle    = {BMC PROCEEDINGS},
  issn         = {1753-6561},
  language     = {eng},
  location     = {Bergen, Norway},
  number       = {suppl. 6},
  pages        = {6},
  title        = {A review of COFRADIC techniques targeting protein N-terminal acetylation},
  url          = {http://dx.doi.org/10.1186/1753-6561-3-S6-S6},
  volume       = {3},
  year         = {2009},
}

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