[Effect of the volumetric dielectric properties of the medium on stability of the globular proteins and membranes].
Analysis of the temperature dependences of the denaturation enthalpy of three domains of albumin molecule showed significant distinctions in the destabilizing effect of ethanol on certain domains of the nondefatted and defatted albumin molecules. A linear relationships were found among the parameters of proteins and membranes stability and bulk dielectric constants of the solvents. It has been suggested that the dielectric characteristics of the medium play a significant role in the maintaining of the certain conformation of proteins and membranes.
Zavodnik
I B
IB
Lapshina
E A
EA
D002152:Calorimetry, Differential Scanning; D004910:Erythrocyte Membrane / Q000737:chemistry; D000431:Ethanol; D005227:Fatty Acids / Q000737:chemistry; D006358:Hot Temperature; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D012709:Serum Albumin / Q000737:chemistry*; D012996:Solutions / Q000737:chemistry; D013816:Thermodynamics
D005227:Fatty Acids; D008565:Membrane Proteins; D012709:Serum Albumin; D012996:Solutions; D000431:Ethanol