Conformation of sarafotoxin-6b in aqueous solution determined by NMR spectroscopy and distance geometry.
The solution structure of sarafotoxin-6b in water has been determined using high-resolution NMR spectroscopy. 127 proton-proton distance measurements and three phi 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 alpha-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.
Mills
R G
RG
Department of Biochemistry, University of Sydney, NSW, Australia.
Atkins
A R
AR
Harvey
T
T
Junius
F K
FK
Smith
R
R
King
G F
GF
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D014757:Viper Venoms / Q000737:chemistry; D014867:Water
D010455:Peptides; D014757:Viper Venoms; C057354:sarafotoxins s6; D014867:Water