Nanodiscs versus Macrodiscs for NMR of Membrane Proteins

被引：74

作者：

Park, Sang Ho ^{[1
]}

Berkamp, Sabrina ^{[1
]}

Cook, Gabriel A. ^{[1
]}

Chan, Michelle K. ^{[1
]}

Viadiu, Hector ^{[1
]}

Opella, Stanley J. ^{[1
]}

机构：

[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

来源：

BIOCHEMISTRY | 2011年 / 50卷 / 42期

基金：

美国国家卫生研究院;

关键词：

PHOSPHOLIPID-BILAYER NANODISCS; FD COAT PROTEIN; STRUCTURAL-ANALYSIS; ALIGNED BICELLES; SPECTROSCOPY; PHOSPHATIDYLCHOLINE; CRYSTALLIZATION;

D O I：

10.1021/bi201289c

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

It is challenging to find membrane mimics that stabilize the native structures, dynamics, and functions of membrane proteins. In a recent advance, nanodiscs have been shown to provide a bilayer environment compatible with solution NMR. We show that increasing the lipid to "belt" peptide ratio expands their diameter, slows their reorientation rate, and allows the protein-containing discs to be aligned in a magnetic field for oriented sample solid-state NMR. The spectroscopic properties of membrane proteins with one to seven transmembrane helices in q = 0.1 isotropic bicelles, similar to 10 nm diameter isotropic nanodiscs, similar to 30 nm diameter magnetically aligned macrodiscs, and q = 5 magnetically aligned bicelles are compared.

引用

页码：8983 / 8985

页数：3

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