期刊
ANNUAL REVIEW OF ANALYTICAL CHEMISTRY, VOL 6
卷 6, 期 -, 页码 305-328出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-anchem-062012-092631
关键词
solid-state NMR; isotopic labeling; proteoliposomes; membrane bilayers; transmembrane helices; GPCRs
资金
- NIAID NIH HHS [P01 AI074805, P01AI074805] Funding Source: Medline
- NIBIB NIH HHS [P41EB002031, R01 EB005161, R01EB005161, P41 EB002031] Funding Source: Medline
- NIGMS NIH HHS [R01 GM099986, R01GM099986, R01GM066978, R01 GM066978] Funding Source: Medline
Many biological membranes consist of 50% or more (by weight) membrane proteins, which constitute approximately one-third of all proteins expressed in biological organisms. Helical membrane proteins function as receptors, enzymes, and transporters, among other unique cellular roles. Additionally, most drugs have membrane proteins as their receptors, notably the superfamily of G protein-coupled receptors with seven transmembrane helices. Determining the structures of membrane proteins is a daunting task because of the effects of the membrane environment; specifically, it has been difficult to combine biologically compatible environments with the requirements for the established methods of structure determination. There is strong motivation to determine the structures in their native phospholipid bilayer environment so that perturbations from nonnatural lipids and phases do not have to be taken into account. At present, the only method that can work with proteins in liquid crystalline phospholipid bilayers is solid-state NMR spectroscopy.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据