Abstract
Allosteric regulation is often viewed as thermodynamic in nature. However, protein internal motions during an enzymatic reaction cycle can slow the hoping processes over numerous potential barriers. We propose that regulating molecules may function by modifying the nonequilibrium protein dynamics. The theory predicts that an enzyme under the new mechanism has a different temperature dependence, waiting time distribution of the turnover cycle, and dynamic fluctuation patterns with and without an effector. Experimental tests of the theory are proposed.
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