Research in the Bowler lab focuses on two areas: protein folding and the relationship between protein conformational dynamics and function. 

Our work on protein folding emphasizes the conformational biases inherent in protein denatured states that bias the free energy landscape of a protein toward its native conformer. The ultimate goal of this research is to understand the physical basis of the protein folding code.    

Our work on the relationship between protein conformational dynamics and function focuses on the structural factors that control access to conformers of mitochondrial cytochrome c  which permit peroxidase activity. Under conditions of oxidative stress cytochrome c oxygenation of the inner mitochondrial membrane lipid, cardiolipin, provides the earliest signal in the intrinsic pathway of apoptosis. A key goal of this work is to understand how cytochrome c has evolved to become a regulatory on/off switch for apoptosis.