[Effect of hydration on the molecular dynamic properties of human serum albumin at low temperatures]

The effect of temperature and hydration on phosphorescence of chromatophores and on saturation curves of ESR spectra of spin labels covalently bound to human serum albumin was studied. It has been shown that at 90-260 degrees K albumin hydration results in intensification of motions of hydrophobic parts with low frequencies (vc less than or equal to 10(3) s-1) and does not affect the motions of hydrophobic and surfacial parts with high frequency.