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[Stability of hydrophobic nuclei of protein molecules depending of the degree of packing].

The values of free energies for the formation of hydrophobic cores with different degree of packing of nonpolar side chains have been calculated. It has been shown that the difference between the values of free energy for tightly packed cores inaccessible to water solvent molecules and the values of free energies for less tightly packed hydrophobic cores whose surface is in contact with the water solvent, is 50-60 kJ/mol and coincides with the value of the enzyme free energy change during its interaction with the substrate.