dorsal/arxiv
View SchemaA non-equilibrium dynamic mechanism for the allosteric effect
| Authors | Jianhua Xing |
|---|---|
| Categories | |
| ArXiv ID | physics/0703089 |
| URL | https://arxiv.org/abs/physics/0703089 |
| DOI | 10.1103/PhysRevLett.99.168103 |
| Journal | Phys. Rev. Lett. 99, 168103 (2007) |
Abstract
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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"abstract": "Allosteric regulation is often viewed as thermodynamic in nature. However\nprotein internal motions during an enzymatic reaction cycle can be slow hopping\nprocesses over numerous potential barriers. We propose that regulating\nmolecules may function by modifying the nonequilibrium protein dynamics. The\ntheory predicts that an enzyme under the new mechanism has different\ntemperature dependence, waiting time distribution of the turnover cycle, and\ndynamic fluctuation patterns with and without effector. Experimental tests of\nthe theory are proposed.",
"arxiv_id": "physics/0703089",
"authors": [
"Jianhua Xing"
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"doi": "10.1103/PhysRevLett.99.168103",
"journal_ref": "Phys. Rev. Lett. 99, 168103 (2007)",
"title": "A non-equilibrium dynamic mechanism for the allosteric effect",
"url": "https://arxiv.org/abs/physics/0703089"
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