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 Förster resonance energy transfer after an abrupt change in solutio...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2003-08, Vol.301 (5637), p.1233-1235
Main Authors: Lipman, Everett A., Schuler, Benjamin, Bakajin, Olgica, Eaton, William A.
Format: Article
Language:English
Subjects:
Bacterial plant pathogens
Bacterial Proteins - chemistry
Biological and medical sciences
Cold Temperature
Conformation
Diffusion
Donors
Dyes
Energy
Energy Transfer
Fluorescence
Fluorescence microscopy
Fluorescence Resonance Energy Transfer
Fundamental and applied biological sciences. Psychology
Kinetics
Laboratory Equipment
Laser beams
Lasers
Materials
Models, Molecular
Molecules
Observation
Pathology. Damages, economic importance
Phytopathology. Animal pests. Plant and forest protection
Plant cells
Population Distribution
Protein Conformation
Protein Denaturation
Protein Folding
Proteins
Technology application
Thermodynamics
Thermotoga maritima - chemistry
Transfer Rates (College)
Virulence
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Summary: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 Förster 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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1085399