Author:
G. Graziano Università del Sannio Dipartimento di Scienze Biologiche ed Ambientali Via Port’Arsa 11 82100 Benevento Italy

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Abstract  

It is shown the non-occurrence of a correlation between the values of the denaturation temperature and those of the denaturation heat capacity change for a set of 13 proteins possessing the ‘SH3-type’ fold from both mesophilic and thermophilic microorganisms. This seems to be a rather general result, because, fixed the size and the folding pattern, the denaturation heat capacity change is a nearly constant quantity, within the uncertainty limits of experimental determinations, regardless of the thermal stability of the protein. A precise definition of the thermodynamics of the hydrophobic effect is presented to clarify that the above finding does not imply that the hydrophobic effect does not play a role in the extra-thermal stability of thermophilic and hyperthermophilic proteins.

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation
1969
Volumes
per Year
1
Issues
per Year
24
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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