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Nuclear magnetic relaxation dispersion profiles in the Larmor frequency range of 0.02-50 MHz and 277 K has been studied for human serum proteins: albumin, γ-globulins and α, β-globulins in aqueous solutions 3-14 per cent by weight of protein. The linear concentration dependences have been found both for the longitudal relaxation rates for water protons and the dispersive and non-dispersive parts of relaxation profiles. The frequency dependent relaxivities have been calculated, the hydrodynamic effect for the albumin macromolecule Brownian rotational correlation time has been observed and analyzed. The importance of molecular weight of protein for the relaxation processes and its influence for magnetic resonance imaging contrast was discussed.