Franzin Carla M, Teriete Peter, Marassi Francesca M
Burnham Institute for Medical Research, La Jolla, CA 92037, USA.
J Am Chem Soc. 2007 Jul 4;129(26):8078-9. doi: 10.1021/ja0728371. Epub 2007 Jun 13.
The anisotropic spin interactions measured for membrane proteins in weakly oriented micelles and in oriented lipid bilayers provide independent and potentially complementary high-resolution restraints for structure determination. Here we show that the membrane protein CHIF adopts a similar structure in lipid micelles and bilayers, allowing the restraints from micelle and bilayer samples to be combined in a complementary fashion to enhance the structural information. Back-calculation and assignment of the NMR spectrum of CHIF in oriented lipid bilayers, from the structure determined in micelles, provides additional restraints for structure determination as well as the global orientation of the protein in the membrane. The combined use of solution and solid-state NMR restraints also affords cross-validation for the structural analysis.
在弱取向胶束和取向脂质双层中测量的膜蛋白各向异性自旋相互作用，为结构测定提供了独立且可能互补的高分辨率约束条件。在这里，我们表明膜蛋白CHIF在脂质胶束和双层中采用相似的结构，使得来自胶束和双层样品的约束条件能够以互补方式相结合，从而增强结构信息。根据在胶束中确定的结构，对取向脂质双层中CHIF的核磁共振谱进行反演和归属，为结构测定以及蛋白质在膜中的整体取向提供了额外的约束条件。溶液核磁共振和固态核磁共振约束条件的联合使用，也为结构分析提供了交叉验证。
