Clusterization of protein molecules in water-salt lisozyme solutions

Electron paramagnetic resonance technique was employed to reveal the nonmonotonous and reversible alterations of the average distance between spin-labeled lysozyme molecules (35 mg/mL.). The changes depend on the NaCl concentration within the range of 0 to 3 mol/L and are parallel to the variations in the solution heterogeneity. The obtained results are interpreted based on the idea of continuous overcritical phase transitions and different types of protein clusters’ development.