[Increase in rigidity of lysozyme molecule during the binding of inhibitors]

An increase in Young's modulus of different solid samples (amorphous and crystalline) of hen egg white lysozyme after soaking them with inhibitor solution was shown to originate from the restriction of domain mobility when the inhibitor binds at the active site cleft provided the binding induces no changes in the packing of the molecules in the samples. N-acetyl-D-glucosomine was found to be able to bind in two sites of the crevice of active centre. The change in the compliance of the globule resulted from the inhibitor binding and low limit of globule compliance was estimated to be 0,14 H-1 m.