AI Article Synopsis
- Conformational switches are macromolecules that can change between two states when they bind to a target molecule, making them useful for biosensors.
- Researchers have developed advanced sensors called conformational rheostat sensors, which improve dynamic range and response time by linking signals to the unfolding process of certain proteins.
- The study focuses on the small α-helical protein BBL, showing it can effectively sense pH and ionic strength with a linear response over four orders of magnitude in concentration and fast response times that are nearly independent of concentration.
Article Abstract
Conformational switches are macromolecules that toggle between two states (active/inactive or folded/unfolded) upon specific binding to a target molecule. These molecular devices provide an excellent scaffold for developing real-time biosensors. Here we take this concept one step beyond to build high-performance conformational rheostat sensors. The rationale is to develop sensors with expanded dynamic range and faster response time by coupling a given signal to the continuous (rather than binary) unfolding process of one-state downhill folding protein modules. As proof of concept we investigate the pH and ionic-strength sensing capabilities of the small α-helical protein BBL. Our results reveal that such a pH/ionic-strength sensor exhibits a linear response over 4 orders of magnitude in analyte concentration, compared to the 2 orders of magnitude for switches, and nearly concentration-independent microsecond response times.
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| http://dx.doi.org/10.1021/ja301092z | DOI Listing |
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