使用粉末样品和旋转扩散确定膜破坏蛋白的取向：一种简单的固态核磁共振方法。
Orientation Determination of Membrane-Disruptive Proteins Using Powder Samples and Rotational Diffusion: A Simple Solid-State NMR Approach.
作者信息
Hong Mei, Doherty Tim
机构信息
Department of Chemistry, Iowa State University, Ames, IA 50011.
出版信息
Chem Phys Lett. 2006 Dec 4;432(1-3):296-300. doi: 10.1016/j.cplett.2006.10.067.
Abstract
The orientation of membrane proteins undergoing fast uniaxial rotation around the bilayer normal can be determined without macroscopic alignment. We show that the motionally averaged powder spectra exhibit their 0° frequency, [Formula: see text], at the same position as the peak of an aligned sample with the alignment axis parallel to the magnetic field. This equivalence is exploited to determine the orientation of a β-sheet antimicrobial peptide not amenable to macroscopic alignment, using (13)CO and (15)N chemical shifts from powder spectra. This powder sample approach permits orientation determination of naturally membrane-disruptive proteins in diverse environments and under magic-angle spinning.
摘要
围绕双层法线进行快速单轴旋转的膜蛋白的取向无需宏观排列即可确定。我们表明，运动平均粉末光谱在与取向轴平行于磁场的排列样品的峰相同位置处显示其0°频率[公式：见正文]。利用这种等效性，使用粉末光谱中的（13）C O和（15）N化学位移来确定不适合宏观排列的β-折叠抗菌肽的取向。这种粉末样品方法允许在不同环境中以及在魔角旋转下确定天然膜破坏蛋白的取向。
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