The conformation of apamin

FEBS Letters

Freeman, C.M.¹  Hider, R.C.²  Catlow, C.R.A.¹  Hemmings, A.M.³ 

[1] Department of Chemistry, University of Keele, Keele ST5 5BG, England;Department of Chemistry, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, England;Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, England

关键词: Apamin Secondary structure Energy minimization;   

DOI  :  10.1016/0014-5793(86)80344-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown