ISSN:
1573-4943
Keywords:
Bacillus thuringiensis
;
toxin
;
secondary structure
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The secondary structure of the toxin fromBacillus 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% α-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% β-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 α-helical and β-sheet structures. No significant differences were detected in the secondary structure of the toxin either in solution or as a hydrated pellet.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01024989
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