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

• Published in: Journal of structural biology Vol. 216; no. 3; p. 108114
• Main Authors: Meshcheryakova, Olga V., Bogdanov, Maxim A., Efimov, Alexander V.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.09.2024
• Subjects: Collagen; Denaturation temperature; Hydrophobic residues; Database; Denaturation temperature; Hydrophobic residues; Collagen
• ISSN: 1047-8477; 1095-8657; 1095-8657
• DOI: 10.1016/j.jsb.2024.108114

[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.