Ultrahigh-resolution (<1.0 Å) structures have revealed unprecedented and unexpected details of molecular geometry, such as the deformation of aromatic rings from planarity. However, the functional utility of such energetically costly strain is unknown. The 0.83 Å structure of α-lytic protease (αLP) indicated that residues surrounding a conserved Phe side-chain dictate a rotamer which results in a ∼6°distortion along the side-chain, estimated to cost 4 kcal∕mol. By contrast, in the closely related protease Str…
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