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. Author manuscript; available in PMC: 2008 Oct 6.
Published in final edited form as: Pharmacol Rev. 2008 Mar 5;60(1):43–78. doi: 10.1124/pr.107.07111

Fig. 7.

Fig. 7

Energy landscape changes upon ligand binding. A, rugged energy landscape of a structurally flexible protein showing many energy minima assigned to conformational substates. Each substate is populated differently. In principle, each of these substates may bind certain specific ligands. B, interactions occurring upon ligand binding change the energy landscape. In some cases new substates may be created and conformational substates that bind the ligand will be favored over substates. Such changes in substates and their populations may modulate protein function and also may lead to protein destabilization and malfunction.