Timothy Cross | Homepage

Professor of Chemistry & Biochemistry

Research Interests

Membrane Protein Structure

Our goal is to characterize the structure and dynamics of membrane proteins for understanding molecular function; in particular we are interested in cation channels. Membrane proteins represent a major challenge for structural biology. Very few structures have been obtained to date, but new methods such as solid state NMR have the potential to be an important technology, complementary to solution state NMR and x-ray crystallography for solving these important drug targets. In previous studies of the channel-forming polypeptide gramicidin A, we have described detailed functional principles that influence conductance efficiency and conductance specificity.

To obtain information for membrane proteins, this laboratory is a world leader in the development of solid-state NMR techniques for structural and dynamic characterizations. Through the use of lipid bilayer preparations that are uniformly aligned with respect to the magnetic field of the NMR spectrometer, it is possible to obtain high-resolution spectra without the required presence of isotropic motions..

Currently, we are working on several membrane proteins. The M2 protein from influenza A virus forms a H+ channel and is a key functional protein in flu infections. Here, our goal is to obtain a complete three-dimensional structure. Another project involves the KcsA K+ channel from Streptomyces lividans.

Teaching

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