期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1865, 期 11, 页码 1512-1521出版社
ELSEVIER
DOI: 10.1016/j.bbapap.2017.08.007
关键词
Rhodopsins; Oligomerization; Folding; Ion transport; Membrane protein structure; Photosensory transduction
资金
- Natural Sciences and Engineering Research Council of Canada (NSERC) [RGPIN-2013-250202, RGPIN-2017-06862]
- Canada Excellence Research Chairs program
- Canadian Institute for Advanced Research (CIFAR)
Retinal-binding proteins, mainly known as rhodopsins, function as photosensors and ion transporters in a wide range of organisms. From halobacterial light-driven proton pump, bacteriorhodopsin, to bovine photoreceptor, visual rhodopsin, they have served as prototypical alpha-helical membrane proteins in a large number of biophysical studies and aided in the development of many cutting-edge techniques of structural biology and biospectroscopy. In the last decade, microbial and animal rhodopsin families have expanded significantly, bringing into play a number of new interesting structures and functions. In this review, we will discuss recent advances in biophysical approaches to retinal-binding proteins, primarily microbial rhodopsins, including those in optical spectroscopy, X-ray crystallography, nuclear magnetic resonance, and electron paramagnetic resonance, as applied to such fundamental biological aspects as protein oligomerization, folding, and structure.
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