[Elastic properties of triclinic crystals of lysozyme in anhydric acetonitrile]

Measurements of lysozyme crystal elastic properties in anhydrous acetonitrile were performed in order to investigate the role of water in protein elasticity. It was shown that triclinic crystals of lysozyme are suitable for such kind of investigation because of being placed in acetonitrile they save crystal lattice parameters. The observed changes of lysozyme crystals elastic properties are close to those found earlier for partially dehydrated protein. These results point to water influence on intramolecular conformational mobility of protein. The water-protein electrostatic interaction and Laplase's pressure as possible mechanisms of this influence are discussed.