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Cysteine Oxidation in Proteins: Structure, Biophysics, and Simulation
Diego Garrido Ruiz1, Angelica Sandoval-Perez1, Amith Vikram Rangarajan1
1Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, United States.
Abstract:
Cysteine side chains can exist in distinct oxidation states depending on the pH and redox potential of the environment, and cysteine oxidation plays important yet complex regulatory roles. Compared with the effects of post-translational modifications such as phosphorylation, the effects of oxidation of cysteine to sulfenic, sulfinic, and sulfonic acid on protein structure and function remain relatively poorly characterized. We present an analysis of the role of cysteine reactivity as a regulatory factor in proteins, emphasizing the interplay between electrostatics and redox potential as key determinants of the resulting oxidation state. A review of current computational approaches suggests underdeveloped areas of research for studying cysteine reactivity through molecular simulations.
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