Thermoimpedancemetric curves of human serum albumin aqueous solutions of various concentrations and pH are obtained. It is shown that the globule-coil transition in individual globules is observed and the curve shape reflects albuminconformational changes including changes under the different denaturants influence. The possibility of denaturation kinetics study by means of thermoimpedancemetry is demonstrated. Results obtained allow to expand diagnostic capabilities of cerebrospinal fluid thermoimpedancemetry on the conformational diseases.