Ion transport proteins are known to be particularly important for the proper functioning of the central nervous system. Ion channel defects are known to cause multiple CMS disorders such as: various types of ataxia, familial hemiplegic migraines, hyperekplexia, and epilepsy (4). By solving the structures of various ion channels, insight into how these channels operate can be gained which will allow for better treatment of disorders resulting from the improper functioning of these channels. For the proposed work, research will be performed on membrane proteins from Mycobacterium tuberculosis. Homology research indicates that there is an evolutionary link between ion transport proteins from bacterial and mammalian cells (5). It is therefore suggested that membrane protein models from this mycobacterium will translate to mammalian models of similar proteins. Multiple alpha-helical membrane proteins will be overexpressed, isolated, purified, and stabilized. Once pure, stable protein has been obtained, backbone membrane protein structure will be determined using a combination of solution and solid state NMR. ? ?

Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Predoctoral Individual National Research Service Award (F31)
Project #
5F31NS054494-02
Application #
7155549
Study Section
Special Emphasis Panel (ZRG1-F04B (20))
Program Officer
Stewart, Randall R
Project Start
2005-12-22
Project End
2008-12-21
Budget Start
2006-12-22
Budget End
2007-12-21
Support Year
2
Fiscal Year
2007
Total Cost
$29,149
Indirect Cost
Name
Florida State University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
790877419
City
Tallahassee
State
FL
Country
United States
Zip Code
32306
Chauhan, Ashwini; Lofton, Hava; Maloney, Erin et al. (2006) Interference of Mycobacterium tuberculosis cell division by Rv2719c, a cell wall hydrolase. Mol Microbiol 62:132-47
Page, Richard C; Moore, Jacob D; Nguyen, Hau B et al. (2006) Comprehensive evaluation of solution nuclear magnetic resonance spectroscopy sample preparation for helical integral membrane proteins. J Struct Funct Genomics 7:51-64