RESUMO
The influence of proteins (bovine serum albumin, BSA, and mouse gamma-globulin, IgG) physically adsorbed or covalently attached via coupling with N-cyclohexyl-N'-(2-morpholinoethyl) carbodiimide methyl-p-toluenesulfonate, CMC, to the surface of activated carbon SCN (spherical carbon with nitrogen) on the mobility of interfacial water molecules was studied by means of 1H NMR spectroscopy with freezing-out of bulk water at 180 < T < 273 K. Relaxation processes in the interfacial non-freezing water were investigated measuring transverse time t2 of proton relaxation dependence on the presence of proteins and CMC. The distribution function of activation free energy of relaxation (with a maximum at 20-22 kJ/mol) was calculated for the protein-water-carbon systems using a regularization procedure and the relationships between t2 and the amounts of the interfacial water unfrozen at T < 250 K assuming the Arrhenius-type dependence for t2(-1) on temperature. The state of unfrozen water in pores of SCN shows that the low temperature relaxation processes occur in narrow pores with half-width X < 1.5 nm.
