Authors:
G. Tsereteli St.Petersburg State University Research Institute of Physics Ulyanovskaya 1 Petergoff 198904 Russia

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T. Belopolskaya St.Petersburg State University Research Institute of Physics Ulyanovskaya 1 Petergoff 198904 Russia

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N. Grunina St.Petersburg State University Research Institute of Physics Ulyanovskaya 1 Petergoff 198904 Russia

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O. Vaveliouk St.Petersburg State University Research Institute of Physics Ulyanovskaya 1 Petergoff 198904 Russia

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Abstract  

By method of differential scanning calorimetry the absolute values of heat capacity for the systemwater–biopolymer (globular and fibrillar proteins and DNA) were measured in a wide range of temperatures (from -30 up to 130°C) and concentrations of proteins both in native and denatured states. Thermal properties of humid denatured biopolymers demonstrate a characteristic anomaly in the form of the heat capacity jump at temperature depending on the bound water content. It has been shown that in the systems studied a glass transition, where water serves as a native plasticizer, is observed. It has been established that the S-shaped character of all heat capacity curves obtained on dehydration for native and denatured biopolymers is due to the gradual transition to the glassy state of both native and denatured samples. It was found that thermally denatured humid small globular proteins at subsequent dissolving in water at room temperature are able to restore their native structure.

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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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