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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Determination of helix-helix interactions in membranes by rotational resonance NMR.
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Determination of helix-helix interactions in membranes by rotational resonance NMR.

机译：通过旋转共振NMR测定膜中的螺旋-螺旋相互作用。

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摘要

Dimerization of human glycophorin A in erythrocyte membranes is mediated by specific interactions within the helical transmembrane domain of the protein. Rotational resonance NMR provides a unique approach for obtaining high-resolution structural data in membrane systems and has been used to establish intermolecular contacts in the glycophorin A dimer by using hydrophobic peptides that correspond to the transmembrane sequence. Magnetization exchange rates were measured between [13C]methyl labels in the hydrophobic sequence -G79-V80-M81-A82-G83-V84- located in the middle of the transmembrane domain and specific [13C]carbonyl labels along the peptide backbone across the dimer interface. Significant magnetization exchange was observed only between V80 (13CH3) and G79 (13C = O) and between V84 (13CH3) and G83 (13C = O), indicating that these residues are packed in the dimer interface in a "ridges-ingrooves" arrangement.
机译：人血红蛋白A在红细胞膜中的二聚化是由蛋白质螺旋跨膜结构域内的特定相互作用介导的。旋转共振NMR为获得膜系统中的高分辨率结构数据提供了一种独特的方法，并且已被用于通过使用与跨膜序列相对应的疏水性肽在糖蛋白A二聚体中建立分子间接触。测量位于跨膜结构域中间的疏水序列-G79-V80-M81-A82-G83-V84-中的[13C]甲基标记与沿着二聚体两端的肽主链的特定[13C]羰基标记之间的磁化交换率接口。仅在V80（13CH3）和G79（13C = O）之间以及V84（13CH3）和G83（13C = O）之间观察到显着的磁化交换，表明这些残基以“脊-齿”排列堆积在二聚体界面中。

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