Artikel ; Online: Cysteine Oxidation in Proteins: Structure, Biophysics, and Simulation.
2022 Band 61, Heft 20, Seite(n) 2165–2176
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 ... ...
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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Mesh-Begriff(e) | Biophysics ; Cysteine/chemistry ; Oxidation-Reduction ; Proteins/chemistry ; Sulfenic Acids ; Sulfonic Acids |
Chemische Substanzen | Proteins ; Sulfenic Acids ; Sulfonic Acids ; Cysteine (K848JZ4886) |
Sprache | Englisch |
Erscheinungsdatum | 2022-09-26 |
Erscheinungsland | United States |
Dokumenttyp | Journal Article ; Review |
ZDB-ID | 1108-3 |
ISSN | 1520-4995 ; 0006-2960 |
ISSN (online) | 1520-4995 |
ISSN | 0006-2960 |
DOI | 10.1021/acs.biochem.2c00349 |
Datenquelle | MEDical Literature Analysis and Retrieval System OnLINE |
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