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Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
Published on: December 20, 2010
Identification of Protein Cysteine Modifications Using Unbiased Mass Spectrometry-Based Proteomics
Mark Schreuder1, Mark Larance2
1School of Life Sciences, University of Technology Sydney and Centenary Institute, University of Sydney, Sydney, NSW, Australia.
Abstract:
Post-translational modifications (PTMs) can play vital roles in the protein's structure, function, localization, and interactions, enabling dynamic control of cellular processes. As such, understanding these modifications is essential to elucidate key biological mechanisms. This chapter discusses an unbiased, mass spectrometry-based approach using wildcard (open) searches in the Byonic platform to detect and identify nondisulfide cysteine PTMs. By targeting individual cysteines and scanning for mass shifts across a broad range, this strategy enables discovery of novel or unexpected modifications. The method is applicable to both new and existing datasets and can be extended to any amino acid, offering a versatile tool for redox and PTM-focused proteomics.

