High-resolution 1H MAS RFDR NMR of biological membranes.
High-resolution 1H MAS RFDR NMR of biological membranes.
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DOI：
10.1016/j.jmr.2008.12.009
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发表时间：
2009-03
期刊：
影响因子：
--
通讯作者：
Smith SO
中科院分区：
文献类型：
--
作者：
Aucoin D;Camenares D;Zhao X;Jung J;Sato T;Smith SO
魔角旋转（MAS）与高分辨率1H NOESY NMR实验相结合，是一种用于测量生物膜中通过空间的1H.1H偶极耦合的既定方法。脂质酰基链的链段运动沿着脂质的整体旋转扩散提供了足够的运动，以将1H偶极相互作用平均到MAS可以有效的范围内。该方法的一个缺点是松弛过程产生显著的串扰强度所需的相对长的NOESY混合时间。为了更快地驱动磁化转移，我们在混合时间期间使用固态射频驱动偶极再耦合（RFDR）脉冲。我们比较了1H MAS NOESY实验与1H MAS RFDR实验二肉豆蔻酰磷酸胆碱，双层形成脂质，并表明，1H MAS RFDR实验提供了相当快的磁化交换比标准的1H MAS NOESY实验。我们应用的方法来模型化合物含有基本的和芳香族的氨基酸结合到膜双层，以说明定位的芳香族基团的位置，已经渗透到下面的脂质头基的水平的能力。
The combination of magic angle spinning (MAS) with the high-resolution 1H NOESY NMR experiment is an established method for measuring through-space 1H…1H dipolar couplings in biological membranes. The segmental motion of the lipid acyl chains along with the overall rotational diffusion of the lipids provides sufficient motion to average the 1H dipolar interaction to within the range where MAS can be effective. One drawback of the approach is the relatively long NOESY mixing times needed for relaxation processes to generate significant crosspeak intensity. In order to drive magnetization transfer more rapidly, we use solid-state radiofrequency driven dipolar recoupling (RFDR) pulses during the mixing time. We compare the 1H MAS NOESY experiment with a 1H MAS RFDR experiment on dimyristoylphosphocholine, a bilayer forming lipid, and show that the 1H MAS RFDR experiment provides considerably faster magnetization exchange than the standard 1H MAS NOESY experiment. We apply the method to model compounds containing basic and aromatic amino acids bound to membrane bilayers to illustrate the ability to locate the position of aromatic groups that have penetrated to below the level of the lipid headgroups.
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