Denaturing and refolding of protein molecules on surfaces.
Denaturing and refolding of protein molecules on surfaces.
复制标题
表面蛋白质分子的变性和重折叠。
DOI：
10.1002/pmic.200700053
复制
发表时间：
2007
期刊：
影响因子：
3.4
通讯作者：
Guo,Athena
中科院分区：
文献类型：
--
作者：
Holtz,Bryan;Wang,Yini;Zhu,Xiao-Yang;Guo,Athena
将蛋白质分子保持在固体表面上的活性状态对于蛋白质微阵列和其他基于蛋白质的生物传感器至关重要。在这里，我们表明，2-D化学环境控制的变性绿色荧光蛋白系固表面的重折叠。在排斥性PEG官能化表面上容易发生重折叠，但在吸引性-NH 2官能化表面上被抑制。这一结果表明了二维化学环境在维持和恢复表面蛋白质活性方面的至关重要性，并为设计用于蛋白质折叠的二维分子伴侣打开了大门。
Keeping protein molecules in the active state on a solid surface is essential to protein microarrays and other protein‐based biosensors. Here, we show that the 2‐D chemical environment controls the refolding of the denatured green fluorescent proteins tethered to solid surfaces. Refolding occurs readily on the repulsive PEG functionalized surface but is inhibited on the attractive –NH2functionalized surface. This result shows the critical importance of the 2‐D chemical environment in the maintenance and revival of protein activity on surfaces and opens the door to designing 2‐D molecular chaperones for protein folding.