期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 129, 期 26, 页码 8078-+出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja0728371
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资金
- NCI NIH HHS [P30 CA030199, R01 CA082864-05, R01 CA082864] Funding Source: Medline
- NIBIB NIH HHS [P41 EB002031] Funding Source: Medline
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.
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