用于磷脂双层中旋转排列膜蛋白的MAS固态NMR的偶极辅助归属协议（DAAP）。
Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.
作者信息
Das Bibhuti B, Zhang Hua, Opella Stanley J
机构信息
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0307, United States.
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0307, United States.
出版信息
J Magn Reson. 2014 May;242:224-32. doi: 10.1016/j.jmr.2014.02.018. Epub 2014 Mar 1.
Abstract
A method for making resonance assignments in magic angle spinning solid-state NMR spectra of membrane proteins that utilizes the range of heteronuclear dipolar coupling frequencies in combination with conventional chemical shift based assignment methods is demonstrated. The Dipolar Assisted Assignment Protocol (DAAP) takes advantage of the rotational alignment of the membrane proteins in liquid crystalline phospholipid bilayers. Improved resolution is obtained by combining the magnetically inequivalent heteronuclear dipolar frequencies with isotropic chemical shift frequencies. Spectra with both dipolar and chemical shift frequency axes assist with resonance assignments. DAAP can be readily extended to three- and four-dimensional experiments and to include both backbone and side chain sites in proteins.
摘要
展示了一种用于膜蛋白魔角旋转固态核磁共振谱共振归属的方法，该方法利用异核偶极耦合频率范围并结合基于传统化学位移的归属方法。偶极辅助归属方案（DAAP）利用了膜蛋白在液晶磷脂双层中的旋转排列。通过将磁不等价的异核偶极频率与各向同性化学位移频率相结合，可获得更高的分辨率。具有偶极和化学位移频率轴的谱图有助于共振归属。DAAP可以很容易地扩展到三维和四维实验，并包括蛋白质中的主链和侧链位点。
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