Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR

被引：10

作者：

Marek, Antonin ^{[1
]}

Tang, Wenxing ^{[1
]}

Milikisiyants, Sergey ^{[1
]}

Nevzorov, Alexander A. ^{[1
]}

Smirnov, Alex I. ^{[1
]}

机构：

[1] N Carolina State Univ, Dept Chem, Raleigh, NC 27695 USA

来源：

BIOPHYSICAL JOURNAL | 2015年 / 108卷 / 01期

基金：

美国国家科学基金会;

关键词：

ALUMINUM-OXIDE NANOPORES; PF1 COAT PROTEIN; PHOSPHOLIPID BICELLES; TRANSMEMBRANE DOMAIN; HYDROPHOBIC MISMATCH; SPECTROSCOPY; DYNAMICS; PHASE; VESICLES; VIRUS;

D O I：

10.1016/j.bpj.2014.11.011

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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 N-15-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.

引用

页码：5 / 9

页数：5

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