The Magic of Bicelles Lights Up Membrane Protein Structure

被引：286

作者：

Duerr, Ulrich H. N. ^{[1
]}

Gildenberg, Melissa ^{[1
]}

Ramamoorthy, Ayyalusamy ^{[1
]}

机构：

[1] Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA

来源：

CHEMICAL REVIEWS | 2012年 / 112卷 / 11期

关键词：

SOLID-STATE NMR; RESIDUAL DIPOLAR COUPLINGS; NUCLEAR-MAGNETIC-RESONANCE; ALIGNED PHOSPHOLIPID-BILAYERS; MYELIN BASIC-PROTEIN; ISLET AMYLOID POLYPEPTIDE; HETERONUCLEAR CORRELATION SPECTROSCOPY; ELECTRON-PARAMAGNETIC-RESONANCE; DIMERIC TRANSMEMBRANE DOMAIN; TWIN-ARGININE TRANSLOCASE;

D O I：

10.1021/cr300061w

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Biological membranes and membrane proteins, responsible for numerous exciting biological processes, present one of the paramount challenges in biophysics today. Membranes are present in great number and variety in all organisms. They form the boundary between the inside and outside for any bacterium or cell, and they delimit the host of organelles that make up their inner subunits. Membranes delimit any cell and all of its compartments. They form natural borders for metabolic substances and signaling molecules. Membrane proteins are the porters and gatekeepers that make sure that only proper molecules or signals make it across the membrane. The number of elucidated structures of membrane proteins has grown exponentially after the first structure was published in 1985, thus equaling the rate at which structure determination of soluble proteins emerged early on. Still, the number of available high-resolution structures of membrane proteins is limited.

引用

页码：6054 / 6074

页数：21

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