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  Experimental and calculated conformational characteristics of the bicyclic heptapeptide phalloidin

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.

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JMolBiol_79_1973_185.pdf (Any fulltext), 2MB
 
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Patel, Dinshaw J., Author
Tonelli, A. E., Author
Pfaender, Peter1, Author           
Faulstich, Heinz2, Author           
Wieland, Theodor1, Author           
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1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              
2Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497703              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 1971-05-161973-05-292004-10-251973-09-05
 Publication Status: Issued
 Pages: 13
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0022-2836(73)90278-7
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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 79 (1) Sequence Number: - Start / End Page: 185 - 196 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042