AI Article Synopsis
- A new method was created to detect fluorescence signals from individual molecules moving in a capillary cell, using a specialized optical system with a spherical mirror for precise measurements.
- The technique includes a "flow-and-stop" control that significantly extends the observation time for single molecules to several seconds, far exceeding traditional confocal methods.
- This approach was applied to study cytochrome c in its unfolded state, revealing detailed time series data that shows different dynamic substates of the proteins on a millisecond scale, offering insights into the protein-folding energy landscape.
Article Abstract
A method was developed to detect fluorescence intensity signals from single molecules diffusing freely in a capillary cell. A unique optical system based on a spherical mirror was designed to enable quantitative detection of the fluorescence intensity. Furthermore, "flow-and-stop" control of the sample can extend the observation time of single molecules to several seconds, which is more than 1000 times longer than the observation time available using a typical confocal method. We used this method to scrutinize the fluorescence time series of the labeled cytochrome c in the unfolded state. Time series analyses of the trajectories based on local equilibrium state analysis revealed dynamically differing substates on a millisecond time scale. This system presents a new avenue for experimental characterization of the protein-folding energy landscape.
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| http://dx.doi.org/10.1021/ja3020555 | DOI Listing |
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