Work

Discovery of lysine post-translational modifications through mass spectrometric detection

Year: 2012

Type: article

Abstract: 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.

Source: Essays in Biochemistry

DOI: 10.1042/bse0520147

Authors: Barry M. Zee, Benjamin A. Garcia

Institution: Princeton University

Language: English

Topic: Advanced Proteomics Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Science Foundation, National Institutes of Health

Award: Novel Methodology for Quantitative High-throughput Cancer Epigenetics