Single-molecule measurement of protein folding kinetics

被引：315

作者：

Lipman, EA

Schuler, B

Bakajin, O

Eaton, WA

机构：

[1] NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA

[2] Lawrence Livermore Natl Lab, Biosecur Nanosci Lab, Livermore, CA 94550 USA

来源：

SCIENCE | 2003年 / 301卷 / 5637期

关键词：

D O I：

10.1126/science.1085399

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

In order to investigate the behavior of single molecules under conditions far from equilibrium, we have coupled a microfabricated laminar-flow mixer to a confocal optical system. This combination enables time-resolved measurement of Forster resonance energy transfer after an abrupt change in solution conditions. Observations of a small protein show the evolution of the intramolecular distance distribution as folding progresses. This technique can expose subpopulations, such as unfolded protein under conditions favoring the native structure, that would be obscured in equilibrium experiments.

引用

页码：1233 / 1235

页数：3

共 21 条

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