Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR
Publication date: 6 January 2015
Source:Biophysical Journal, Volume 108, Issue 1
Author(s): Antonin Marek , Wenxing Tang , Sergey Milikisiyants , Alexander*A. Nevzorov , Alex*I. Smirnov
Anodic aluminum oxide substrates with macroscopically aligned homogeneous nanopores of 80*nm in diameter enable two-dimensional, solid-state nuclear magnetic resonance studies of lipid-induced conformational changes of uniformly 15N-labeled Pf1 coat protein in native-like bilayers. The Pf1 helix tilt angles in bilayers composed of two different lipids are not*entirely governed by the membrane thickness but could be rationalized by hydrophobic interactions of lysines at the bilayer interface. The anodic aluminum oxide alignment method is applicable to a broader repertoire of lipids versus bicelle bilayer mimetics currently employed in solid-state nuclear magnetic resonance of oriented samples, thus allowing for elucidation of the role played by lipids in shaping membrane proteins.
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