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Electron paramagnetic resonance signal parameters of TEMPO dichlorotriazineand TEMPO maleimide spin labels attached to protein human serum albuminmolecules have been monitored at various temperatures, salts and sucroseconcentrations. The method for measuring the correlation time of the proteinrotational dynamics using viscosity isotherms was utilized. The correlationtime is proportional to the effective protein volume dependent on proteinstructure dynamic stability in a certain temperature range which can thus bedetermined. Sharp temperature changes in the effective volume and theirdependence on the concentration of NaCl, ammonium sulphate, polyethyleneglycol, and heavy water are interpreted as interconversions of stable low andhightemperature protein conformers with the participation of intermediates. Fewvariants of the qualitative phase diagrams of water-salt dispersion of theprotein were presented on the basis of the results obtained. The regions havebeen marked, where thermo and salt induced liquid liquid phase transitions canoccur, as well as intermediates and supramolecular structures of the proteincan form in their course.

Spin labeling -- electron paramagnetic resonance spectroscopy study of temperature and salt dependent serum albumin stability