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Computational Modeling of Lysine Post-Translational Modification: An Overview

Md. Mehedi Hasan , Mst. Shamima Khatun, and Hiroyuki Kurata

Living organisms have a magnificent ordered and complex structure. In regulating the cellular functions, post-translational modifications (PTMs) are critical molecular measures. They alter protein conformation, modulating their activity, stability and localization. Up to date, more than 300 types of PTMs are experimentally discovered in vivo and in vitro pathways [1,2]. Major and common PTMs are methylation, ubiquitination, succinylation, phosphorylation, glycosylation, acetylation, and sumoylation. PTM is a biological mechanism common to both prokaryotic and eukaryotic organisms, which controls the protein functions and stability or the proteolytic cleavage of regulatory subunits and affects all aspects of cellular life. The PTM of a protein can also determine the cell signaling state, turnover, localization, and interactions with other proteins [3]. Therefore, the analysis of proteins and their PTMs are particularly important for the study of heart disease, cancer, neurodegenerative diseases and diabetes [4,5]. Since the characterization of PTMs gets invaluable insight into the cellular functions in etiological processes, there are still challenges. Specifically, the major challenges in studying PTMs are the development of specific detection and purification methods.