Research at the intersection between metabolites and proteins
We are passionate about using modern mass spectrometry techniques to probe how proteins and metabolites work together to react to various cellular stressors. Specifically, we use native mass spectrometry and proteomics in conjunction with LC/MS-based metabolomics to study how thiol and redox metabolism or oxidative phosphorylation (OXPHOS) can directly modulate protein function and how vitamins are metabolized into key protein cofactors.
Thiol Redox Regulation
Thiols, or sulfur-containing molecules span from small to large biomolecules and regulate key biological processes ranging from cardiovascular disease to cancer. We study how thiol metabolism can modulate enzymatic function through post-translational modification on cysteine residues.
Vitamin/Cofactor Metabolism
Vitamins are necessary molecules in our diet and often function as enzyme cofactors. We examine how vitamin availability is regulated by metabolism and how vitamin-cofactor loading can modulate protein function.
Complex Consequences of OXPHOS
Oxidative phosphorylation (OXPHOS) is a highly dynamic pathway that generates the majority of cellular energy and is located in the mitochondria. We focus on how OXPHOS function can directly affect enzyme and protein activity through noncovalent interactions and posttranslational modifications.
