Solution conformation of leiurotoxin I (scyllatoxin) by 1H nuclear magnetic resonance

Abstract
A proton NMR study at 500 MHz of leiurotoxin I in water is presented. Nearly complete sequence‐specific assignments of the individual backbone and side‐chain proton resonances were achieved using through‐bond and through‐space connectivities obtained from standard two‐dimensional NMR techniques. The secondary structure of this toxin is inferred from a combination of short‐range nuclear Overhauser enhancements, scalar couplings and proton/deuteron exchange rates. Three disulflde bridges locate the N‐terminal part (that is α‐helical from residue 6 to 16) on one side of a C‐terminal two stranded antiparallel β sheet (from Leu18 to Val29). The latter features a tight turn at Gly23‐Asp24.

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