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

Olga V Meshcheryakova; Maxim A Bogdanov; Alexander V Efimov

doi:10.1016/j.jsb.2024.108114

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

J Struct Biol. 2024 Sep;216(3):108114. doi: 10.1016/j.jsb.2024.108114. Epub 2024 Jul 31.

Authors

Olga V Meshcheryakova¹, Maxim A Bogdanov², Alexander V Efimov³

Affiliations

¹ Centre for Biomedical Research of the Karelian Research Centre of the Russian Academy of Sciences, Pushkinskaya St., 11, Petrozavodsk 185910 Russia. Electronic address: mesch@krc.karelia.ru.
² Laboratory of Intellectual Services and Applications, ITMO University, Kronverksky Pr., 49, St.Petersburg 197101, Russia.
³ Institute of Protein Research, Russian Academy of Sciences, Institutskaya St., 4, Pushchino, Moscow Region 142290 Russia. Electronic address: efimov@protres.ru.

PMID: 39094716
DOI: 10.1016/j.jsb.2024.108114

Abstract

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 (T_m) or denaturation temperature (T_d) 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.

Keywords: Collagen; Database; Denaturation temperature; Hydrophobic residues.

MeSH terms

Collagen* / chemistry
Hydrophobic and Hydrophilic Interactions*
Protein Denaturation*
Protein Stability*
Temperature
Transition Temperature

Substances

Collagen