Collagen-DNA macromolecular complex study by the proton magnetic   relaxation method
  Comparing the obtained experimental data for the proton magnetic relaxation with the microcalorimetric ones it is concluded that in the aqueous solution of collagen + DNA at temperatures below 35oC a stable molecular complex collagen-DNA is formed prohibiting the formation of the hydration cover of collagen which is manifested by the almost two times decrease of hydration. At temperatures (25-45)oC the disruption of complex and melting of triple helix of collagen takes place. Starting from temperature 45oC up to 90oC hydration values, calculated from experimental data on proton relaxation for solution and, theoretical values calculated for the solution coincide speaking of the fact that macromolecules in the solution are not practically interacting with each other and not influencing the creation of each others hydration covers. 
G.M.Mrevlishvili, D.V.Svintradze, N.O.Dzhariashvili,   L.O.Namisheishvili, G.I.Mamniashvili, Yu.G.Sharimanov, T.O.Gegechkori