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RESEARCH FRONT
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
+ Author Affiliations
- Author Affiliations

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




Armand G. Ngounou Wetie received his diploma in biotechnology (2008) from the Mannheim University of Applied Sciences, Germany, and a Master of Science degree in molecular biotechnology from the Technical University of Munich (TUM), Germany. Currently, Armand is a Ph.D. student in the Department of Chemistry and Biomolecular Science at Clarkson University (Potsdam, New York), where he is working on understanding the mode of action of the tumour differentiation factor (TDF) protein.


Izabela Sokolowska received her M.Sc. in biotechnology at Warsaw University of Life Sciences (2009) and currently she is a Ph.D. student in the Biochemistry and Proteomics Group at Clarkson University. Her research is focussed on the characterisation of newly discovered protein tumour differentiation factors (TDF) and mass spectrometry-based approaches in the analysis of proteins.


Dr Alisa Woods is a neurobiologist and mental health counsellor, and currently Research Assistant Professor in the Department of Chemistry and Biomolecular Science at Clarkson University, as well as Counsellor and Neuropsychology Researcher at the Neuropsychology Clinic/Psychoeducation Services, SUNY Plattsburgh, New York. The long-term goal of her research is to understand the connections between biochemistry and behaviour in neurodevelopmental disorders, including autism and ADHD. She is particularly interested in the identification of protein biomarkers for diagnosis and prognosis of neurodevelopmental disorders, and in their use for monitoring the psychotherapeutic/behavioural treatment of developmental disorders.


Dr Costel C. Darie is a biochemist and currently Assistant Professor and leader of the Biochemistry and Proteomics Group within the Department of Chemistry and Biomolecular Science at Clarkson University. He received his B.S. and M.S. in biochemistry from Iasi, Romania, and his Ph.D. in biochemistry from Freiburg, Germany. Dr Darie's main research interests are in new proteomics approaches for biomarker discovery and identification of post-translational modifications and protein–protein interactions. His research is also focussed on the investigation of one particular protein – the tumour differentiation factor protein.

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

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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