1H‐NMR study of gramicidin A transmembrane ion channel

FEBS Letters

Ovchinnikov, Yu.A.¹  Lomize, A.L.¹  Arseniev, A.S.¹  Bystrov, V.F.¹  Barsukov, I.L.¹ 

[1] Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Ul. Miklukho-Maklaya, 16/10, Moscow V-437, USSR

关键词: Gramicidin A;    Ion channel;    NMR;    Nuclear Overhauser effect;    Peptide conformation;    Single-stranded helix;   

DOI  :  10.1016/0014-5793(85)80702-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structure of[Val¹]gramicidin A incorporated into sodium dodecyl-d ₂₅ sulphate micelles has been studied by two-dimensional proton NMR spectroscopy. Analysis of nuclear Overhauser effects, spin-spin couplings and solvent accessibility of NH groups show that the conformation of the Na⁺ complex of gramicidin A in detergent micelles, which in many ways mimic the phospholipid bilayer of biomembranes, is an N-terminal to N-terminal (head-to-head) dimer formed by two right-handed, single-stranded β^6.3 helices with 6.3 residues per turn, differing from Urry's structure by handedness of the helices.

【 授权许可】

Unknown