Abstract
Energy minimisation techniques are used as a tool to distinguish between different proposed models for the structure of the bee venom polypeptide apamin. The influence of electrostatic interactions on the resultant energies is noted. The model of Hider and Ragnarsson [(1980) FEBS Lett. 111, 189-193] is found to be of consistently low energy.
Original language | English |
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Pages (from-to) | 289-296 |
Number of pages | 8 |
Journal | FEBS Letters |
Volume | 197 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 3 Mar 1986 |
Externally published | Yes |
Keywords
- Apamin Secondary structure Energy minimization