Hongjun Liang

Research Associate

Education

• Ph.D. from the University of Illinois at Urbana-Champaign, 2005
• M.S. from the Institute of Chemistry, Chinese Academy of Sciences, 1998
• B.S. from the University of Science and Technology of China, 1995

Research: Directed Assembly of Membrane Proteins

Membrane proteins (MPs) are a class of nanoscopic entities that control the matter, energy, and information transport across cellular boundaries. Directional reconstitution of detergent-purified MPs into well-ordered 2-D or 3-D arrays is notoriously difficult. Proteorhodopsin is the MP used by marine bacterioplankton as a light-driven proton pump, and is postulated to function photophysiologically for global energy and matter transformations. We demonstrated a rapid cooperative assembly process directed by universal electrostatic interactions that spontaneously organizes proteorhodopsin molecules into 2-D or 3-D ordered crystalline arrays with well-defined orientation and packing density, and identified a charge density matching mechanism that selectively controls the assembly process. Understanding this rapid electrostatically driven assembly process sheds light on organizing MPs in general, which is a prerequisite for their structural and mechanistic studies as well as many in vitro applications.

Publications

1. H. J. Liang, G. Whited, C. Nguyen, A. Okerlund, and G. D. Stucky, Inherently Tunable Electrostatic Assembly of Membrane Proteins., Nano Lett, in press (2007)
2. H. J. Liang, G. Whited, C. Nguyen, and G. D. Stucky, The directed cooperative assembly of proteorhodopsin into 2D and 3D polarized arrays, Proc. Natl. Acad. Sci. U. S. A. 104, 8212-8217 (2007)
3. H. J. Liang, G. Whited, and G. D. Stucky, Membrane Protein Arrays and Methods of Making Thereof, provisional US patent, application no. 60/849,993 (2006)

Contact

hliang [at] chem.ucsb.edu