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Secondary structure of ShK toxin, a potassium-channel-blocking peptide (1996)

Kem, William R. ; Sanyal, Gautam ; Williams, Robert W. ; [et al.]

Springer

International journal of peptide research and therapeutics 3 (1996), S. 69-72

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ISSN: 1573-3904

Keywords: Peptide ; Secondary structure ; Raman ; CD ; Potassium-channel toxin ; Sea anemone

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology

Notes: Summary 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% β-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 Ala14 through Leu25 is predicted.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00126735

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