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Funding News - Research on the Structural Biology of Membrane Proteins Sought

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The National Institute of Neurological Disorders and Stroke (NINDS) encourages applications for basic research on the structures of membrane proteins at atomic resolution. This announcement is made together with 8 other components of the National Institutes of Health (NIH). *

Membrane proteins play a crucial role in many cellular and physiological processes. They are essential mediators of material and information transfer between cells and their environment, between compartments within cells, and between compartments comprising the organ systems. Despite the importance of membrane proteins, the knowledge of their high-resolution structures and mechanisms of action has lagged far behind the knowledge of their properties in general.

Examples of research areas of interest include: methods for over-expression of native and modified membrane proteins; methods for isolation, purification, and stabilization of membrane proteins, including the development of new detergent and non-detergent solubilization agents; methods for crystallization of membrane proteins and crystal manipulation that could facilitate data collection; methods for electron diffraction, particularly for the production of suitable 2D-crystals; methods for nuclear magnetic resonance (NMR) analysis of membrane proteins in solution, in micelles, and in their native lipid environments; and methods to elucidate the organization of lipid and detergent molecules within protein crystalline arrays.

For more information, potential applicants should contact Dr. Randall Stewart, Program Director, Channels, Synapses and Circuits Cluster, NINDS, Neuroscience Center, 6001 Executive Boulevard, Room 2135, Bethesda, MD 20892; telephone: 301-496-1917; fax: 301-402-1501; e-mail: stewartr@ninds.nih.gov.

*: For a full list of supporting NIH components and a more detailed description of this program announcement, please visit the NIH web site at: http://grants.nih.gov/grants/guide/pa-files/PA-02-060.html.