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EnglishHere we report the first results of combined scanning calorimetric and dilatometric investigations carried out on bovine serum albumin in aqueous solution at 30-97°C. Comparison of experimental data obtained by the two techniques suggests a "steps" model for the thermal denaturation of the protein. Moreover, the results in the high-temperature region, after aggregation of the unfolded chain, show a subsequent, previously unreported, spatial rearrangement of the polypeptidic chain network, during which the order of the system increases with an increase in temperature. The results indicate that scanning dilatometry is a very useful method of detecting phenomena which are not seen by calorimetry. The results also demonstrate the determinant role of water in the unfolding process. © 1994.
| Titolo: | A combined scanning dilatometric and differential scanning calorimetric study of the thermal unfolding of bovine serum albumin | |
| Autori interni: | ||
| Data di pubblicazione: | 1994 | |
| Rivista: | ||
| Handle: | http://hdl.handle.net/20.500.11769/357863 | |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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