Relationship between thermal stability of collagens and the fraction of hydrophobic residues in their molecules

[Display omitted] •Database of the thermal stability of collagens (1200 records, about 340 animal species).•Calculation of the number of hydrophobic residues in collagens.•Thermostability of collagens depends on the fraction of hydrophobic residues in their molecules. In this study, a database of th...

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Bibliographic Details
Published in:Journal of structural biology 2024-09, Vol.216 (3), p.108114, Article 108114
Main Authors: Meshcheryakova, Olga V., Bogdanov, Maxim A., Efimov, Alexander V.
Format: Article
Language:English
Subjects:
Collagen
Denaturation temperature
Hydrophobic residues
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Summary:[Display omitted] •Database of the thermal stability of collagens (1200 records, about 340 animal species).•Calculation of the number of hydrophobic residues in collagens.•Thermostability of collagens depends on the fraction of hydrophobic residues in their molecules. In this study, a database of the thermal stability of collagens and their synthetic analogues has been compiled taking into account literature sources. In total, our database includes 1200 records. As a result of a comparative theoretical analysis of the collected experimental data, the relationship between the melting temperature (Tm) or denaturation temperature (Td) of collagens and the fraction of hydrophobic residues (f) in their molecules has been established. It is shown that this relationship is linear: the larger the f value, the higher the denaturation or melting temperature of a given collagen.
ISSN:1047-8477
1095-8657
1095-8657
DOI:10.1016/j.jsb.2024.108114