期刊
BIOPHYSICAL JOURNAL
卷 88, 期 3, 页码 1932-1947出版社
CELL PRESS
DOI: 10.1529/biophysj.104.044412
关键词
-
类别
The three amino acids S65, T203, and E222 crucially determine the photophysical behavior of wild-type green fluorescent protein. We investigate the impact of four point mutations at these positions and their respective combinations on green fluorescent protein`s photophysics using absorption spectroscopy, as well as steady-state and time-resolved fluorescence spectroscopy. Our results highlight the influence of the protein's hydrogen-bonding network on the equilibrium between the different chromophore states and on the efficiency of the excited-state proton transfer. The mutagenic approach allows us to separate different mechanisms responsible for fluorescence quenching, some of which were previously discussed theoretically. Our results will be useful for the development of new strategies for the generation of auto fluorescent proteins with specific photophysical properties. One example presented here is a variant exhibiting uncommon blue fluorescence.
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