Author/Editor | Kranjc, Zdenka; Lapanje, Savo; Poklar, Nataša | |
Title | Circular dichroic studies of thermal denaturation and denaturation by urea and alkylureas of human serum albumin | |
Type | članek | |
Source | Acta Chim Slov | |
Vol. and No. | Letnik 41, št. 3 | |
Publication year | 1994 | |
Volume | str. 279-94 | |
Language | eng | |
Abstract | The thermal denaturation of human serum albumin was investigated by measurement of circular dichroism (CD). On the basis of CD spectra secondary structure in the temperature range 25 - 85 degrees C was calculated. Solvent denaturation of the same protein by urea and some alkylureas (methyl-, ethyl- and N.N'-dimethylurea) was also studied by the sametechnique and secondary structure in 0 - 9 M solutions was ascertained. The results obtained indicate dependence of molar ellipticity on the alkyl group in urea molecule. Moreover, by using the data obtained and the assumption of two-state transition native - denatured protein, a thermodynamic analysis of the process is feasible and apparent thermodynamic quantities. Gibbs free energy, enthalphy and entropy of transition were obtained. Comparison of these values with those obtained by calorimetry shows that the apparent quantities are much smaller which indicates that the thermal denaturation of human serum albumin in water is a multi-state transition. | |
Descriptors | SERUM ALBUMIN CIRCULAR DICHROISM PROTEIN DENATURATION UREA TEMPERATURE THERMODYNAMICS PROTEIN STRUCTURE, SECONDARY |