The TEMPO Group is dedicated to experimental and molecular dynamics studies of membranes and membrane proteins. The Group is comprised of the members of the laboratories of Stephen White, Jim Hall, Francesco Tombola (Physiology and Biophysics), Douglas Tobias (Chemistry), Melanie Cocco (Molecular Biology and Biochemistry), and Rachel W. Martin (Chemistry).

The broad goal of our research is to elucidate the physicochemical principles that determine the folding and stability of proteins in membranes, and apply the insight gained to the development of tools for predicting the structures of membrane proteins. We explore how Molecular Dynamics (MD) simulations can be used in conjunction with experimental controls to gain knowledge and develop insights about biomacromolecular systems.

The image at the top of this page is a snapshot from a molecular dynamics simulation of the CLC chloride channel protein of E. Coli in a POPC lipid bilayer (Freites et al. 2004), based on the 2.5  Å resolution structure reported by Dutzler, R. et al. (2003). The protein channel is shown in orange in secondary structure representation according to STRIDE (Frishman and Argos, 1995). Lipid headgroups are in red, lipid acyl chains are in gray, and waters are shown in cyan. The image was made with VMD (Humphrey et al. 1996).