Physics – Biological Physics
Scientific paper
2007-03-07
Phys. Rev. Lett. 99, 168103 (2007)
Physics
Biological Physics
accepted by Phys. Rev. Lett. Major revisions were made to fit the style. 4 pages, 2 figures
Scientific paper
10.1103/PhysRevLett.99.168103
Allosteric regulation is often viewed as thermodynamic in nature. However protein internal motions during an enzymatic reaction cycle can be slow hopping 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 different temperature dependence, waiting time distribution of the turnover cycle, and dynamic fluctuation patterns with and without effector. Experimental tests of the theory are proposed.
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