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Article << Previous     |     Next >>   Contents Vol 66(7)

Identification of Post-Translational Modifications by Mass Spectrometry

Armand G. Ngounou Wetie A , Izabela Sokolowska A , Alisa G. Woods A B and Costel C. Darie A C

A Biochemistry and Proteomics Group, Department of Chemistry and Biomolecular Science, Clarkson University, 8 Clarkson Avenue, Potsdam, NY, 13699-5810, USA.
B Neuropsychology Clinic and Psychoeducation Services, SUNY Plattsburgh, Plattsburgh, NY, 12901, USA.
C Corresponding author. Email: cdarie@clarkson.edu

Australian Journal of Chemistry 66(7) 734-748 http://dx.doi.org/10.1071/CH13144
Submitted: 30 March 2013  Accepted: 17 May 2013   Published: 1 July 2013


 
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Abstract

Proteins are the effector molecules of many cellular and biological processes and are thus very dynamic and flexible. Regulation of protein activity, structure, stability, and turnover is in part controlled by their post-translational modifications (PTMs). Common PTMs of proteins include phosphorylation, glycosylation, methylation, ubiquitination, acetylation, and oxidation. Understanding the biology of protein PTMs can help elucidate the mechanisms of many pathological conditions and provide opportunities for prevention, diagnostics, and treatment of these disorders. Prior to the era of proteomics, it was standard to use chemistry methods for the identification of protein modifications. With advancements in proteomic technologies, mass spectrometry has become the method of choice for the analysis of protein PTMs. In this brief review, we will highlight the biochemistry of PTMs with an emphasis on mass spectrometry.





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