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The conformation of apamin
Author(s) -
Freeman C.M.,
Catlow C.R.A.,
Hemmings A.M.,
Hider R.C.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80344-1
Subject(s) - apamin , chemistry , biophysics , biology , potassium channel
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.