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In this paper we try to perform a thermodynamic analysis of the temperature-induced transition from the molten globule to the unfolded state of globular proteins. A series of calorimetric investigations showed that this process is not associated with an excess heat capacity absorption peak, and cannot be regarded as a first-order phase transition. This result contrasts with the well-established conclusion that the thermal unfolding of the native tertiary structure of globular proteins is a first-order phase transition. First, the theoretical approach developed by Ikegami is outlined to emphasize that a second-order or gradual transition induced by temperature is expected for globular proteins when the various secondary structure elements do not interact cooperatively. Secondly, a simple thermodynamic model is presented which, taking into account the independence of the secondary structure elements among each other, is able to rationalize the shape of the experimental DSC profiles.

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  • Impact Factor (2019): 2.731
  • Scimago Journal Rank (2019): 0.415
  • SJR Hirsch-Index (2019): 87
  • SJR Quartile Score (2019): Q3 Condensed Matter Physics
  • SJR Quartile Score (2019): Q3 Physical and Theoretical Chemistry
  • Impact Factor (2018): 2.471
  • Scimago Journal Rank (2018): 0.634
  • SJR Hirsch-Index (2018): 78
  • SJR Quartile Score (2018): Q2 Condensed Matter Physics
  • SJR Quartile Score (2018): Q2 Physical and Theoretical Chemistry

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