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　allosteric　drug　design.　In　the　present　work,　a　thermodynamic　method　based　on　the　elastic　network　model　was　proposed　to　predict　the　allosteric　sites　on　the　protein　surface.　In　our　method,　the　thermodynamic　coupling　between　the　allosteric　and　active　sites　was　considered,　and　then　the　allosteric　sites　were　identified　as　those　where　the　binding　of　an　effector　molecule　induces　a　large　change　in　the　binding　free　energy　of　the　protein　with　its　ligand.　Using　the　proposed　method,　two　proteins,　i.e.,　the　70　kD　heat　shock　protein　(Hsp70)　and　GluA2　alpha-amino-3-hydroxy-5-methyl-4-isoxazole　propionic　acid　(AMPA)　receptor,　were　studied　and　the　allosteric　sites　on　the　protein　surface　were　successfully　identified.　The　predicted　results　are　consistent　with　the　available　experimental　data,　which　indicates　that　our　method　is　a　simple　yet　effective　approach　for　the　identification　of　allosteric　sites　on　proteins.