creator Chang, Shih-chia advisor Howard, Andrew J Cholera is a severe disease that causes devastating diarrhea when Vibrio cholerae infects the human intestine. Once the bacterium gets the access into the intestinal cell, adenosine diphosphate (ADP)- ribosylation of the human signaling protein Gs!!is catalyzed by the cholera toxin A1 subunit (CTA1). According to the previous researches, this reaction is activated allosterically by a GTP-bound human ADP-ribosylation factor six (ARF6). Arginine is one of the substrates for cholera toxin A1 subunit. In the thesis, the crystal structure of agmatine, a L-arginine analogue, bound to the protein complex of the mutant CTA1 with ARF6-GTP reveals the possibility of how arginine might interact with the complex. Submitted by Dana Lamparello (dlampare@iit.edu) on 2013-03-01T22:11:18Z No. of bitstreams: 1 FinalThesis.pdf: 4157175 bytes, checksum: 6c5c56ca6ad5b2cfea6de7a172d08121 (MD5) Made available in DSpace on 2013-03-01T22:11:18Z (GMT). No. of bitstreams: 1 FinalThesis.pdf: 4157175 bytes, checksum: 6c5c56ca6ad5b2cfea6de7a172d08121 (MD5) Previous issue date: 2012-07 M.S. in Molecular Biochemistry and Biophysics, July 2012 2012-07-12 2012-07 http://hdl.handle.net/10560/2897 en Thesis born digital application/pdf In Copyright http://rightsstatements.org/page/InC/1.0/ Restricted Access BIOL / Biology Illinois Institute of Technology Affiliated department