Conformation of sarafotoxin‐6b in aqueous solution determined by NMR spectroscopy and distance geometry

FEBS Letters

Junius, F.Keith³  Atkins, Annette R.¹  Harvey, Tim²  Smith, Ross¹  Mills, Robyn G.³  King, Glenn F.³ 

[1] Department of Biochemistry, University of Queensland, Qld 4072, Australia;Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK;Department of Biochemistry, University of Sydney, NSW 2006, Australia

关键词: Sarafotoxin;    Endothelin;    NMR;    Protein Structure;    Bronchoconstriction;    Distance Geometry;    NMR;    nuclear magnetic resonance;    ET-1;    endothelin-1;    DMSO;    dimethylsulphoxide;    S6b;    sarafotoxin-6b;    DG;    distance geometry;    RMD;    restrained molecular dynamics;    CD;    circular dichroism;    FID;    free induction decay;    TPPI;    time proportional phase incrementation;    2D HOHAHA;    two-dimensional homonuclear Hartmann Hahn spectroscopy;    2D DQF-COSY;    two-dimensional double quantum filtered correlated spectroscopy;    rf;    radio-frequency;    2D NOESY;    two-dimensional nuclear Overhauser effect spectroscopy;    τm;    mixing period in NOESY experiment;    τc;    temperature relaxation time of bath;    Δ l;    time step;    K dc;    force constant for NMR restraints;    αCH;    α-carbon proton;    NH;    amide proton;    βCH;    β-carbon proton;    RMSD;    root mean square deviation;    nOe;    nuclear Overhauser effect;   

DOI  :  10.1016/0014-5793(91)80488-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown