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Chhowalla Group Research
Gold Nanoparticles (acquired by UltraSTEM)
hybrid perovskite single crystals
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Fabris Group Research

Development of Biofunctional Interfaces for Templated Protein Crystallization & Membrane Protein-based Sensing

Categories: Chemistry and Chemical Biology (CCB)
Speaker: David Thompson, Purdue University
Date & Time: October 6, 2009 - 11:00am
Location: W/R Auditorium

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 [4] 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 [10]. 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.

[1] J Biol Chem 1998 273, 7177-7180.
[2] Chem Lett 2007 36, 956-975.
[3] Supramol Chem 2005 17, 101-111.
[4] J Am Chem Soc 2008 130, 14076-14077.
[5] Biochemistry 2006 45, 14683-14694.
[6] J Am Chem Soc 2008 130, 4584-4585.
[7] Biophys J 2009, in press.
[8] Langmuir 2007 23, 6276-6280.
[9] Langmuir 2007 23, 6281-6288.
[10] Angew Chem Int Ed 2008 47, 1051-1053.

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