Protein Crystallization at Nanostructured Interfaces. We are exploring the effects of interfacial structure and dynamics on the assembly of two-dimensional protein crystals with an eye toward forging an understanding of the basic principles involved in nucleating the crystallization of soluble proteins. This goal is being pursued using His-tag proteins and a library of non-covalent, amphiphilic nitrilotriacetic acid (NTA) chelating lipids that have been deposited at liquid-solid interfaces [1-3]. These materials can promote the development of long-range order through a site-hopping diffusion mechanism. Opportunities for initiating epitaxial protein crystal growth in this manner and rapidly detecting crystal formation  will be described.
Supported Membrane Sensor Development. Ste14p is a yeast isoprenylcysteine methyltransferase (ICMT), an integral membrane protein involved in K-Ras methylation. Since K-Ras is mutated in many human cancers, an ICMT-based sensor could serve as an important new tool for discovering new inhibitors that target this enzyme. The activity of Ste14p in C20BAS and related C32-based bolalipid membranes for supported membrane sensor applications has been evaluated [5-7] and new strategies for immobilizing the enzyme [8,9] and detecting ICMT activity have been developed . The design principles elaborated by this project could potentially be generalized for many different classes of membrane proteins, including sensory elements, energy-coupled directional transporters, and the recognition domains of infectious agents.
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