Engineering and design of repeat proteins

BIOT 427

Lynne Regan, lynne.regan@yale.edu, Departments of Molecular Biophysics & Biochemistry and Department of Chemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06511, Aitziber Lopez Cortajarena, lynne.regan@yale.edu, MB&B, Yale University, New Haven, CT 06511, and Gilad Haran, Department of Chemical Physics, Weizman Institute, Rehovot, Israel.
Tetratricopeptide Repeat (TPR) proteins provide a perfect scaffold of the engineering and design of proteins with enhanced properties, including stability, supramolecular structure and binding activities. The modular, repetitive nature of repeat proteins in general, and TPR proteins in particular, make them especially suited for rational re-engineering for a variety of applications. Here we present our recent work on the folding and stability of repeat proteins, which allows us to re-design their properties in a ration fashion. We also presnt our recent work on the incorporation of novel activities onto the TPR framework, and show how such novel proteins can be developed for a variety of applications.