Protein post-translational modifications (PTMs) refer to the covalent addition of functional groups onto a protein. They offer another dimension to the functional diversity of the proteins and allow them to do chemistry that is otherwise difficult. Thus, a deeper understanding on the regulatory mechanism of different PTMs can provide critical insights into various underlying cellular processes. In this talk, I will share two PTM-related stories from a chemical biology standpoint.

Structure and function of proteins in aqueous medium can be altered by the presence of cosolvents such as salts or osmolytes (osmoytes: small organic compounds which maintain cellular osmotic stress). Denaturing osmolytes such as urea or denaturing salts such as guanidinium chloride (GdmCl) destabilize the functional conformations of the cellular proteins. In contrast, protein protective osmolytes such as trimethylamine N-oxide (TMAO) stabilize proteins’ native structures. In cellular environment, proteins are exposed to mixtures of many cosolvents.

Abstract