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J Protein Chem. 1990 Feb;9(1):87-94.

Secondary structure of the entomocidal toxin from Bacillus thuringiensis subsp. kurstaki HD-73.

Author information

1
Department of Chemistry, University of Ottawa, Ontario, Canada.

Abstract

The secondary structure of the toxin from Bacillus thuringiensis subsp. kurstaki (Btk) HD-73 was estimated by Raman, infrared, and circular dichroism spectroscopy, and by predictive methods. Circular dichroism and infrared spectroscopy gave an estimate of 33-40% alpha-helix, whereas Raman and predictive methods gave approximately 20%. Raman and circular dichroism spectra, as well as predictive methods, indicated that the toxin contains 32-40% beta-sheet structure, whereas infrared spectroscopy gave a slightly lower estimate. Thus, all of these approaches are in agreement that the native conformation of Btk HD-73 toxin is highly folded and contains considerable amounts of both alpha-helical and beta-sheet structures. No significant differences were detected in the secondary structure of the toxin either in solution or as a hydrated pellet.

PMID:
2340079
[Indexed for MEDLINE]

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