http://www.cnr.it/ontology/cnr/individuo/prodotto/ID218072
A combined scanning dilatometric and differential scanning calorimetric study of the thermal unfolding of bovine serum albumin (Articolo in rivista)
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- Label
- A combined scanning dilatometric and differential scanning calorimetric study of the thermal unfolding of bovine serum albumin (Articolo in rivista) (literal)
- Anno
- 1994-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/0040-6031(94)85168-9 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- C. LA ROSA; MILARDI D; S. FASONE AND D. GRASSO (literal)
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- Rivista
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- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- C. LA ROSA; MILARDI D; S. FASONE AND D. GRASSO, Università degli Studi di Catania, Dipartimento di Scienze Chimiche. (literal)
- Titolo
- A combined scanning dilatometric and differential scanning calorimetric study of the thermal unfolding of bovine serum albumin (literal)
- Abstract
- Here we report the first results of combined scanning calorimetric and dilatometric investigations carried out on bovine serum albumin in aqueous solution at 30-97-degrees-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. (literal)
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