[Thermodynamic properties of biopolymers in spiral and coiled states in the 4--400 degree K temperature interval].

Possibilities of the adiabatic calorimetry methods in the studies of the biopolymer conformational properties in the wide temperature range including helium temperatures are considered. The low temperature peculiarities of the heat capacity difference for the biopolymers being in helical and coiled states are found. It was shown, that in the presence of biomacromolecules the water in the ice-water phase transition region suffers gradual over the temperature phase transition "order-disorder". It was found, that thermodynamic properties of the linear fibrillar structures over the wide temperature range (including helium temperatures) are essentially defined by the state of molecule solvent built-in the biopolymer helical structure. New data on the interaction mechanisms of dissolved salt ions with the biomacromolecules in the native and denaturated states have been obtained. It is shown that the existence of different fractions of bound water with biopolymer is a fact. A conclusion was made that it is necessary to take into account the data on the thermodynamic properties of biomacromolecules and the water bound to them at low temperatures in order to described completely the conformational properties of biomacromolecules.