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Quantifying reversible oxidation of proteins thiols in Chlamydomonas reinhardtii

Undergraduates: Kylie Lawrence, Evan McConnell


Faculty Advisor: Leslie Hicks
Department: Chemistry


Photosynthetic organisms use dynamic post-translational modifications to survive and adapt, which include reversible oxidative modifications of protein thiols that regulate enzymatic structure, function, and activity. This is particularly relevant for Chlamydomonas reinhardtii, a model alga for the study of photosynthesis and biofuel production. Identification of reversible oxidation sites are key, therefore, to maximize production by improving fitness and stress adaptability. Since reversibly oxidized thiols are substoichiometric and perturbed by experimental conditions, measurements of proteinaceous cysteines have been difficult to obtain. The optimization of a method for highly efficient and specific enrichment of reversibly oxidized cysteine residues from intact proteins is described.

 

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