Single-molecule measurement of protein folding kinetics
- 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 Foerster 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.
| Author details: | Everett A. Lipman, Benjamin Schuler, Olgica Bakajin, William A. Eaton |
|---|---|
| URL: | http://www.sciencemag.org/content/301/5637/1233 |
| ISSN: | 0036-8075 |
| Publication type: | Article |
| Language: | English |
| Year of first publication: | 2003 |
| Publication year: | 2003 |
| Release date: | 2017/03/25 |
| Source: | Science. - ISSN 0036-8075. - 301 (2003), 5637, S. 1233 - 1235 |
| Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
