The solution structure of sarafotoxin-6b in water has been determined using high-resolution NMR spectroscopy, 127 proton-proton distance measurements and three ω dihedral angle constraints derived from NMR spectra were used to calculate the solution structure using a combination of distance geometry and restrained molecular dynamics. The major structural feature of the resulting family of five structures was a right-handed α-helix extending from K9 to Q17. In contrast, the C-terminal region of the peptide appears not to adopt a preferred conformation in aqueous solution. The present structure is compared with those previously determined for endothelin peptides in non-aqueous solvents. © 1991.
Mills, R. G., Atkins, A. R., Harvey, T., Junius, F. K., Smith, R., & King, G. F. (1991). Conformation of sarafotoxin-6b in aqueous solution determined by NMR spectroscopy and distance geometry. FEBS Letters, 282(2), 247–252. https://doi.org/10.1016/0014-5793(91)80488-O