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Allostery is a rapid and efficient way in many biological processes to regulate protein functions,where binding of an effector at the allosteric site alters the activity and function at a distant active site.Allosteric regulation of protein biological functions provides a promising strategy for novel drug design.However, how to effectively identify the allosteric sites remains one of the major challenges for the allosteric drug design.In the present work, a thermodynamic method based on the elastic network model was proposed to predict the allosteric sites on protein surface.