Li Junbei, Qiu Xiaoyan J
Jiangsu Key Laboratory of Translational Research and Therapy for Neuro-Psycho-Diseases and College of Pharmaceutical Sciences, Soochow University , Suzhou, Jiangsu 215123, China.
Biochemistry. 2017 Apr 11;56(14):1951-1954. doi: 10.1021/acs.biochem.7b00009. Epub 2017 Apr 3.
For many membrane proteins, self-association serves both structural and functional roles. Studies of such association can be simplified by switching to micelles as the membrane-mimicking environment, but native interaction is not preserved in all detergents. The selection of suitable conditions for biochemical experiments would be greatly facilitated by a quantitative high-throughput assay. Here we showed that the fluorescence polarization reduction, which resulted from homo-Förster resonance energy transfer and was measured in a high-throughput compatible format, can be used to determine both association states and constants for membrane proteins in micelles.
对于许多膜蛋白而言，自我缔合具有结构和功能双重作用。通过改用胶束作为膜模拟环境，此类缔合的研究可以得到简化，但并非所有去污剂都能保留天然相互作用。定量高通量检测将极大地有助于为生化实验选择合适的条件。在此我们表明，由同源Förster共振能量转移导致并以高通量兼容形式测量的荧光偏振降低，可用于确定胶束中膜蛋白的缔合状态和常数。
