CRYSTAL STRUCTURE OF AN ARTIFICIAL 4-HELIX BUNDLE PROTEIN. Christian E. Schafmeister, Sherry LaPorte, Robert M. Stroud, 83 Behr Ave. San Francisco, CA

A 108 residue artificial protein has been designed, expressed, characterized, crystallized and its three dimensional structure has been solved to 2.9 Å resolution. The protein was designed by connecting four identical [[alpha]] helices together with short glycine loops. The component helices are modeled after amphipathic helices which interact with each other through flat hydrophobic faces. This 4-helix bundle is the first crystal structure to reveal an ordered, entirely de novo designed protein motif. This motif offers a template for the design of functionality into a 4-helix bundle protein.