The research in my laboratory focuses on understanding the structural and thermodynamic mechanisms by which proteins perform mechanical activities on a molecular scale, with a long-term goal of developing protein machines with novel activities. Biochemical mechanisms designed to achieve mechanical work rely on the interconversion of meta-stable protein structures in a process that is gated by protein-protein or protein-ligand interactions and coupled to some source of free energy such as high-energy phosphodiester bonds or a concentration gradient. Understanding these mechanisms in detail requires knowledge of the three-dimensional structures of the protein domains and the protein-protein and protein-ligand interfaces, as well knowledge of the thermodynamic stablility of the various conformational states along the reaction pathway and the kinetics with which these states are interconverted. Therefore, research in this area lies at the intersection of the fields of protein structure, molecular recognition, and protein dynamics. The tools that are employed in these studies include high-resolution x-ray crystallography to establish static structures and various forms of protein spectroscopy to characterize the kinetics and thermodynamics of complex formation as well as conformational reaction dynamics.