Discovery of lysine post-translational modifications through mass spectrometric detection.
The complexity of an organism's proteome is in part due to the diversity of post-translational modifications present that can direct the location and function of a protein. To address the growing interest in characterizing these modifications, mass spectrometric-based proteomics has emerged as one of the most essential experimental platforms for their discovery. In searching for post-translational modifications within a target set of proteins to global surveys of particularly modified proteins within a given proteome, various experimental MS (mass spectrometry) and allied techniques have been developed. Out of 20 naturally encoded amino acids, lysine is essentially the most highly post-translationally modified residue. This chapter provides a succinct overview of such methods for the characterization of protein lysine modifications as broadly classified, such as methylation and ubiquitination.
Department of Molecular Biology, Princeton University, Princeton, NJ 08540, U.S.A.
Barry M
BM
Zee
Benjamin A
BA
Garcia
D000818:Animals; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D013058:Mass Spectrometry; D008745:Methylation; D011499:Protein Processing, Post-Translational; D054875:Ubiquitination
D008239:Lysine