Publication Date:
2003-08-30
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lipman, Everett A -- Schuler, Benjamin -- Bakajin, Olgica -- Eaton, William A -- New York, N.Y. -- Science. 2003 Aug 29;301(5637):1233-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, Building 5, Room 104, National Institutes of Health, Bethesda, MD 20892-0520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12947198" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Proteins/*chemistry
;
Cold Temperature
;
Diffusion
;
Energy Transfer
;
Fluorescence
;
Fluorescence Resonance Energy Transfer
;
Kinetics
;
Models, Molecular
;
Protein Conformation
;
Protein Denaturation
;
*Protein Folding
;
Thermodynamics
;
Thermotoga maritima/*chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
