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Mass Spectrometry: Applications in Phosphoproteomics

  1. Francesco Giorgianni1,
  2. Sarka Beranova-Giorgianni2

Published Online: 15 AUG 2008

DOI: 10.1002/9780470048672.wecb304

Wiley Encyclopedia of Chemical Biology

Wiley Encyclopedia of Chemical Biology

How to Cite

Giorgianni, F. and Beranova-Giorgianni, S. 2008. Mass Spectrometry: Applications in Phosphoproteomics. Wiley Encyclopedia of Chemical Biology. 1–8.

Author Information

  1. 1

    The University of Tennessee Health Science Center, Charles B. Stout Neuroscience Mass Spectrometry Laboratory, Memphis, Tennessee

  2. 2

    The University of Tennessee Health Science Center, Department of Pharmaceutical Sciences, Memphis, Tennessee

Publication History

  1. Published Online: 15 AUG 2008

Abstract

Proteins are biological macromolecules whose structure and functions are essential to every biological process within cells. Protein phosphorylation is one of the most important post-translational modifications and it has a profound effect on protein function. Recently, concurrent advances in bioanalytical technologies and informatics enabled studies of proteins and phosphoproteins on a global scale. These large-scale approaches represent an integral component of systems biology, which is an area of scientific inquiry that focuses on a biological system as a whole. State-of-the art mass spectrometry is a key technology for global-scale protein and phosphoprotein analyses. Phosphorylated proteins from diverse biological systems can be probed with a combination of separation methods, tandem mass spectrometry, and bioinformatics, to reveal the identity of the phosphorylated protein and the exact localization of the site(s) of phosphorylation. Characterization of the phosphoproteomes in cells, tissues and biological fluids provides an excellent foundation on which to build new knowledge of living systems.