[Thermal restructuring and hydration of serum albumin].
Calorimetry and dielectrometry in the millimeter wave range have been applied to demonstrate a possibility for determination of heat capacity of bound water in biopolymer matrices in solution is shown. Variation of the hydration level of human serum albumin caused by the variation of temperature and protein concentration is described. Application of two methods based on comparison of calorimetric and dielectric data on protein solutions at different temperatures and concentrations have produced similar values of the heat capacity of bound water in the protein hydration shell (approximately 3 J/g.K).
Gasan
A I
AI
Kashpur
V A
VA
Maleev
V Ia
VIa
D001704:Biopolymers; D002151:Calorimetry; D004560:Electricity; D006358:Hot Temperature; D006801:Humans; D012709:Serum Albumin / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D001704:Biopolymers; D012709:Serum Albumin; D014867:Water
Termicheskie perestroĭki i gidratsiia syvorotochnogo al'bumina.