The paper presents concentration and temperature interrelationships of relaxation parameters in hydrated CC400 protein preparation. Investigations were conducted within the range of concentrations from 0.08 g g-1 to 0.21 g g-1 and the range of temperatures from 20oC to 60oC. On the basis of concentration investigations, the hydration value of the preparation was determined and it was found to amount to 0.20 g per 1 g of non-hydrated preparation and did not depend on temperature. Temperature experiments allowed determining the temperature of the phase transition of the hydrated preparation. This temperature amounted to 39oC. The molecular dynamics was studied analysing the parameter proportional to the average reorientation correlation time of water molecules. It was found that, at the concentration of 0.12 g g-1, the correlation time was the longest, which testifies to the constraint of the dynamics of water molecules in the system. Restriction of the molecule rotation at that concentration indicates that the developed gel was the strongest.