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Experimental and calculated conformational characteristics of the bicyclic heptapeptide phalloidin

MPG-Autoren
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Pfaender,  Peter
Max Planck Institute for Medical Research, Max Planck Society;

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Faulstich,  Heinz
Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society;

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Wieland,  Theodor
Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Patel, D. J., Tonelli, A. E., Pfaender, P., Faulstich, H., & Wieland, T. (1973). Experimental and calculated conformational characteristics of the bicyclic heptapeptide phalloidin. Journal of Molecular Biology (London), 79(1), 185-196. doi:10.1016/0022-2836(73)90278-7.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-002D-9E95-E
Zusammenfassung
Several conformations generated from approximate potential energy calculations are presented for the bicyclic heptapeptide phalloidin which are consistent with the conformation-dependent information obtained from proton nuclear magnetic resonance measurements performed on phalloidin in dimethylsulfoxide solution. In each conformation, the cysteine amide proton is intramolecularly hydrogen bonded, the tryptophan amide is internally buried and the methyl group of the alanine residue preceding tryptophan is shielded by the tryptophan ring. Thus, phalloidin appears to be a relatively rigid molecule in solution.