Specific Lipid Binding of Membrane Proteins in Detergent Micelles Characterized by NMR and Molecular Dynamics.
作者： Linlin Zhao , Shuqing Wang , Changqing Run , Bo OuYang , James J. Chou
DOI: 10.1021/ACS.BIOCHEM.6B00836
关键词:
摘要: Many membrane proteins bind specifically to lipids as an integral component of their structures. The ability detergents support lipid binding is thus important consideration when solubilizing for structural studies. In particular, the zwitterionic phosphocholine (PC)-based detergents, which have been widely used in solution NMR studies channels and transporters, are controversial because strong solubilization power perceived more denaturing than nonionic such maltosides. Here, we investigate mitochondrial ADP/ATP carrier (AAC) cardiolipin, a function, dodecylphosphocholine (DPC) micelles. We found that DPC, AAC binds cardiolipin manner consistent with bound cardiolipins crystal structures determined n-decyl β-d-maltoside. Our results suggest PC detergent compatible specific bi...
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