Andronesi Ovidiu C, Becker Stefan, Seidel Karsten, Heise Henrike, Young Howard S, Baldus Marc
Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
J Am Chem Soc. 2005 Sep 21;127(37):12965-74. doi: 10.1021/ja0530164.
It is shown that molecular structure and dynamics of a uniformly labeled membrane protein can be studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments are combined with novel through-bond correlation schemes that probe mobile protein segments. These NMR schemes are demonstrated on a uniformly [13C,15N] variant of the 52-residue polypeptide phospholamban. When reconstituted in lipid bilayers, the NMR data are consistent with an alpha-helical trans-membrane segment and a cytoplasmic domain that exhibits a high degree of structural disorder.
结果表明，在魔角旋转条件下可以研究均匀标记的膜蛋白的分子结构和动力学。为此，将偶极重耦合实验与探测可移动蛋白片段的新型键连相关方案相结合。这些核磁共振方案在由52个残基组成的多肽受磷蛋白的均匀[13C,15N]变体上得到了验证。当重构于脂质双层中时，核磁共振数据与一个α螺旋跨膜片段和一个高度结构无序的胞质结构域一致。
