Abstract
The temperature dependences of heat capacity for water–denaturated biopolymer (globular proteins, collagen and DNA) were measured in a wide range of temperatures (0–140°C) and water content of the systems. It has been shown that thermally denaturated globular proteins (lysozyme, myoglobin and catalase) are able to form the thermoreversible heat-set structures under the certain conditions studied. The additional endothermal maximum observed is the calorimetric manifestation of the phase transition related to the melting of these thermotropic non-native structures. The melting gels are completely formed just after denaturation during relatively short time and only their prolonged state at T>T d leads to their transformation to thermoirreversible non-melting ones. The post denaturated structures from water-denaturated protein (Mb, Lys and RN-ase) systems with a different amount of free water were also studied. The thermoreversible cold-set gels are formed from both water-denaturated DNA and water-denaturated collagen systems. These thermotropic structures are metastable. A spatial gel network of both collagen and DNA is formed from the native-like renaturated structures.
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Belopolskaya, T.V., Tsereteli, G.I., Grunina, N.A. et al. DSC Study of the Postdenaturated Structures in Biopolymer–water Systems. Journal of Thermal Analysis and Calorimetry 62, 75–88 (2000). https://doi.org/10.1023/A:1010158610943
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DOI: https://doi.org/10.1023/A:1010158610943