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Secondary structure of ShK toxin, a potassium-channel-blocking peptide

✍ Scribed by William R. Kem; Gautam Sanyal; Robert W. Williams; Michael W. Pennington

Publisher: Springer Netherlands
Year: 1996
Tongue: English
Weight: 265 KB
Volume: 3
Category: Article
ISSN: 1573-3149
DOI: 10.1007/bf00126735

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✦ Synopsis

Sea anemones possess small K-channel-blocking peptides about the same size as the scorpion K-channel toxins. We have estimated the secondary structure content (33% helix, 26% ]3-sheet) of one of these toxins, ShK toxin, using CD, Raman, and FTIR spectroscopy. A hypothetical 3D structure of the peptide core has been constructed using secondary structure and disulfide-linkage constraints; a single helical segment running from Ala 14 through Leu 25 is predicted.

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