Direct characterization of protein oligomers and their quaternary structures by single-molecule FRET
Cheolhee Kim1, Jae Yeol Kim, Seung Hyeon Kim
1Department of Physics and School of Interdisciplinary Bioscience & Bioengineering, Pohang University of Science and Technology, Pohang 790-784, South Korea.
Chemical Communications (Cambridge, England)
|December 14, 2011
Abstract:
Using a single-molecule method, we directly distinguish among oligomers from monomers to tetramers and determine their quaternary structures. Using this method, we found that RecR forms a stable dimer and its oligomeric form is modulated by its own concentration and the interaction with RecO.
Related Concept Videos
01:22Protein Folding
Overview
01:19Protein Dynamics in Living Cells
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...