The weekly seminar series organized by CNT and the Molecular Engineering and Sciences Institute provides a forum for bringing national and international leaders in nanoscale science and technology to campus, and for graduate students enrolled in our Dual Ph.D. program in Nanotechnology to present their research.
All seminars are held on Tuesdays from 2:30 to 3:20 PM in Johnson Hall Room 102 (North end of building and across from MolE).
The University of Washington is committed to providing access, equal opportunity and reasonable accommodation in its services, programs, activities, education and employment for individuals with disabilities. To request disability accommodation contact the Disability Services Office at least ten days in advance at: (206) 543-6450/V, (206) 543-6452/TTY, (206) 685-7264 (FAX), or email@example.com.
Structural and functional studies of membrane proteins using cryoEM and nanomaterials
Asst. Prof. Liguo Wang, University of Washington - Biological Structures
Membrane proteins are involved in many critical biological processes, and 70% of all known drug targets are membrane proteins. However, fewer than 300 unique membrane protein structures have been identified. The lack of membrane protein structures hinders the understanding of biological reactions at a molecular level and the development of membrane protein drug discovery. This gap is mainly due to the difficulty in forming crystals for X-ray crystallography. Recently, single-particle cryo-electron microscopy (cryoEM) has been used to study structures of membrane proteins solubilized in detergents. However, both structural and functional studies show the essential role of lipid membrane environments. Here a new method have been developed to study structures and functions of membrane proteins in lipid membranes. This new method employs nanomaterials to restore the lipid membrane environment and to provide the built-in reference for image quality control. This also makes it possible to carry out both structural and functional study of the same sample under the same condition, which allows direct correlations between the 3D molecular structure and the quantitative measurement of the activity of membrane proteins.
Copyright © 2012 The Center for Nanotechnology at the University of Washington