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• W2051230841 startingPage "1213" @default.
• W2051230841 abstract "Neurotoxic peptides from venoms of scorpions and honey bees exhibit a consensus pattern in the two disulfide bridgings related to the sequence portions Cys-X-Cys and Cys-X-X-X-Cys. A revised three-dimensional structure of charybdotoxin, as determined by two-dimensional nmr spectroscopy, confirms that the consensus cystine dislocation generates in all these toxins a common structural element, i.e., the cystine-stabilized alpha-helical (CSH) motif, which may be correlated with their common ion channel blocking activity." @default.
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• W2051230841 date "1991-09-01" @default.
• W2051230841 modified "2023-09-23" @default.
• W2051230841 title "The cystine-stabilized ?-helix: A common structural motif of ion-channel blocking neurotoxic peptides" @default.
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• W2051230841 doi "https://doi.org/10.1002/bip.360311009" @default.
• W2051230841 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1724185" @default.
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