Nature Methods
- 4, 798 - 806 (2007)
Published online: 27 September 2007; | doi:10.1038/nmeth1100
Mapping protein post-translational modifications with mass spectrometryEric S Witze1, 3, William M Old1, 3, Katheryn A Resing1 & Natalie G Ahn1, 21
Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado at Boulder, Boulder, Colorado 80309-0215, USA. 2
Howard Hughes Medical Institute, University of Colorado at Boulder, Boulder, Colorado 80309-0215, USA. 3
These authors contributed equally to this work.
Correspondence should be addressed to Natalie G Ahn natalie.ahn@colorado.edu Post-translational modifications of proteins control many biological processes, and examining their diversity is critical for understanding mechanisms of cell regulation. Mass spectrometry is a fundamental tool for detecting and mapping covalent modifications and quantifying their changes. Modern approaches have made large-scale experiments possible, screening complex mixtures of proteins for alterations in chemical modifications. By profiling protein chemistries, biologists can gain deeper insight into biological control. The aim of this review is introduce biologists to current strategies in mass spectrometry–based proteomics that are used to characterize protein post-translational modifications, noting strengths and shortcomings of various approaches.
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