Proteins are the workhorse macromolecules of the cell, yet mRNA translation to generate the proteome is often not the final step required to yield functional proteins. Over 200 different chemotypes of covalent posttranslational modifications (PTMs) have been characterized to date. These modifications diversify the proteome imparting diverse functional consequences. Another mode of post-translational regulation of proteins is the acquisition of metal ions. An estimated 1/3 to 1/2 of proteins are characterized as metalloproteins requiring binding of metal ion(s) for protein function. Though these phenomena are traditionally studied separately, they are not independent.

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The Ge group is interested in the chemistry and biology of modified proteins, specifically the crosstalk between covalent protein posttranslational modifications (PTMs) and metal binding, and how this crosstalk contributes to human health and the development of disease states such as cancer and neurodegeneration.