Protein engineering of extremophilic chaperones for molecular self-assembly

BIOT 431

Timothy A. Whitehead, taw@berkeley.edu and Douglas S Clark, clark@cchem.berkeley.edu. Department of Chemical Engineering, University of California, Berkeley, 210 Gilman Hall, Berkeley, CA 94720
Self-assembled proteins hold tremendous promise for creating a range of useful nanoscaled templates. Advantages of protein templates include processing in aqueous environments and functionalization through standard genetic engineering to incorporate new chemistries, to embed enzymes, or to incorporate nucleating peptides for a diverse range of inorganic materials. In this talk, we describe the creation of specifically interacting proteins for ordered architectures through the application of powerful genetic selection technology. These architectures are based on the quaternary structure of a new type of filament protein (the γ prefoldin, or γ-PFD) from the hyperthermophile Methanocaldococcus jannaschii that we have previously discovered and characterized. These engineered filaments are to be used as building blocks for 3-D architectures of arbitrary geometry, and progress towards this end will be discussed.