title: Solution structure of apamin determined by nuclear magnetic resonance and distance geometry.
abstract: The solution structure of the bee venom neurotoxin apamin has been determined with a distance geometry program using distance constraints derived from NMR. Twenty embedded structures were generated and refined by using the program DSPACE. After error minimization using both conjugate gradient and dynamics algorithms, six structures had very low residual error. Comparisons of these show that the backbone of the peptide is quite well-defined with the largest rms difference between backbone atoms in these structures of 1.34 A. The side chains have far fewer constraints and show greater variability in their positions. The structure derived here is generally consistent with the qualitative model previously described, with most differences occurring in the loop between the beta-turn (residues 2-5) and the C-terminal alpha-helix (residues 9-17). Comparisons are made with previously derived models from NMR data and other methods.
authors.affiliation: Department of Chemistry, Lawrence Berkeley Laboratory, University of California, Berkeley, California 94720.
authors.forename: J H
authors.initials: JH
authors.lastname: Pease
authors.forename: D E
authors.initials: DE
authors.lastname: Wemmer
mesh_terms: D000465:Algorithms; D001030:Apamin; D001514:Bee Venoms; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015394:Molecular Structure; D012984:Software
chemical_list: D001514:Bee Venoms; D001030:Apamin