F-NMR studies on Anthrax protective antigen -- Restricted access to full text

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Chadegani, Fatemeh
Mulangi, Vennela
Miyagi, Masaru
Bann, James G.

Fatemeh Chadegani, Vennela Mulangi, Masaru Miyagi, and James G. Bann. (2012). F-NMR studies on Anthrax Protective Antigen. -- In Proceedings: 8th Annual Symposium: Graduate Research and Scholarly Projects. Wichita, KS: Wichita State University, p.63-64


Anthrax secretes a three component which is composed of three proteins: lethal factor (LF), edema factor (EF), and protective antigen (PA). PA transfers LF and EF into the host cytosol through a membrane spanning pore, which forms within low pH endosomes. Once EF and LF have entered the cytosol, the enzymatic activities block processes important to the host immune response. We biosynthetically labeled all seven tryptophans in PA with 5-fluorotryptophan to examine the structure of protective antigen using 19F-NMR spectroscopy. We have accomplished NMR experiments as a function of pH (8 to 5) to study the structure of PA. We also carried out temperature and binding studies with the goal of assigning these residues.

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Paper presented to the 8th Annual Symposium on Graduate Research and Scholarly Projects (GRASP) held at the Marcus Welcome Center, Wichita State University, April 18, 2012.
Research completed at the Departments of Chemistry, Wichita State University and 2Case Center for Proteomics and Bioinformatics School of Medicine, Case Western Reserve University