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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.

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Metadaten
Author:Everett A. Lipman, Benjamin Schuler, Olgica Bakajin, William A. Eaton
URL:http://www.sciencemag.org/content/301/5637/1233
ISSN:0036-8075
Document Type:Article
Language:English
Year of first Publication:2003
Year of Completion: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