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Proteins that show similarity in their equil. Since the introduction of the first ENM by Monique Tirion in , several variants using coarser protein models have been proposed and their reliability for the description of protein intrinsic dynamics has been widely demonstrated. Although the concept of induced fit has been widely adopted for describing the structural changes that accompany ligand binding, there is growing evidence in support of the dominance of protein intrinsic dynamics which has been evolutionarily optimized to accommodate its functional interactions. The U-shaped active sites differ mainly due to hydrophobic residues of the substrate channel. We note that the catalytic sites lie at the interface between anticorrelated regions indicated by black lines and red arrows in panel a , again a feature typical of the catalytic site of enzymes e. For inducing structural changes, synthesis of a particular product may not be so important as the ability to induce what amts. To account for natural selection we assume a single active conformation and use basic statistical physics to derive a linear relationship between site-specific evolutionary rates and the local stress of the mutant's active conformation.

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