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The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis δ-endotoxin are consistent with an “umbrella-like” structure of the pore

The aim of this study was to elucidate the mechanism of membrane insertion and the structural organization of pores formed by Bacillus thuringiensis δ-endotoxin. We determined the relative affinities for membranes of peptides corresponding to the seven helices that compose the toxin pore-forming dom...

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Bibliografische gegevens
Hoofdauteurs: Gazit, Ehud, Rocca, Paolo La, Sansom, Mark S. P., Shai, Yechiel
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: The National Academy of Sciences 1998
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC22824/
https://ncbi.nlm.nih.gov/pubmed/9770479
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