Date of Award
1998
Document Type
Thesis
Publication Status
Version of Record
Submission Date
October 2026
Thesis/Dissertation Advisor [Chair]
Mari, Frank
Abstract
The alpha-conotoxin EI is an 18-residue peptide (RDOCCYHPTCNMSNPQIC; 4-10, 5-18) isolated from the venom of Conus ermineus. This peptide targets the nicotinic acetylcholine receptor (nAChR) found in mammalian skeletal muscle and the electric organ of Torpedo. 2D-NMR methods and dynamical simulated annealing protocols have been used to determine the 3D structure of EI. 133 NOE-derived distances were used to produce 13 structures with minimum energy that complied with the NOE restraints. The structure of EI is characterized by a helical loop between T9 and M12 that is stabilized by the C4-C10 disulfide bond and turns involving C4-C5 and N14-P15. The overall fold of EI is similar to that of other alpha4/7 conotoxins (PnIA/B, MII, EpI). However, unlike these other alpha4/7 conotoxins, EI targets the muscular type nAChR. The differences in selectivity can be attributed to the surface charge distribution among these alpha4/7 conotoxins.
Extent
80 p.
Recommended Citation
Franco, Aldo, "Three-dimensional structure of the alpha-conotoxin EI determined by proton NMR spectroscopy" (1998). Electronic Theses and Dissertations 1990 - 1999. 1381.
https://digitalcommons.fau.edu/etd_general_4/1381
Identifier
FADT15609
Comments
Thesis (M.S.)--Florida Atlantic University, 1998.|Thesis (M.S.)--Florida Atlantic University, 1998.