Frank Gabriel A, Kipnis Yakov, Smolensky Elena, Daube Shirley S, Horovitz Amnon, Haran Gilad
Department of Chemical Physics, Weizmann Institute of Science, Rehovot 76100, Israel.
Bioconjug Chem. 2008 Jul;19(7):1339-41. doi: 10.1021/bc800118j. Epub 2008 Jun 24.
We describe the design of an optical switch in the chaperonin GroEL that is opened and closed by its ATP- and cochaperonin GroES-driven conformational changes. The switch, based on a fluorophore and a quencher, is engineered into the single-ring variant of the chaperone, and shows dramatic modulation of its fluorescent intensity in response to the transition of the protein between its allosteric states. It, therefore, forms a sensitive probe for the dynamics of the allosteric transitions of this machine, both in the bulk and in single molecules.
我们描述了伴侣蛋白GroEL中一种光开关的设计,该光开关通过其ATP和共伴侣蛋白GroES驱动的构象变化来打开和关闭。这种基于荧光团和猝灭剂的开关被设计到伴侣蛋白的单环变体中,并在蛋白质在其变构状态之间转变时,显示出荧光强度的显著调制。因此,它构成了一种灵敏的探针,可用于研究该分子机器在整体和单分子水平上变构转变的动力学。