Fiche publication
Date publication
janvier 2026
Journal
Methods in molecular biology (Clifton, N.J.)
Auteurs
Membres identifiés du Cancéropôle Est :
Pr BAUD Stéphanie
Tous les auteurs :
Msoili Z, Wong H, Baud S
Lien Pubmed
Résumé
Modeling of fibrillar collagen such as type I collagen is challenging mainly due to the large size of this protein, its peculiar secondary structure of polyproline II type, found mainly in extracellular matrix proteins, and the presence of posttranslational modifications essential to its function. In this chapter, we present a protocol that allows us to model, at the atomic level, the three-dimensional structure of type I collagen with the THeBuScr and SIDEpro software. The resulting conformation could be used for further molecular docking or molecular dynamics investigations.
Mots clés
Collagen, Fibrillar, Molecular modeling, Posttranslational modification, SIDEpro, THeBuscr
Référence
Methods Mol Biol. 2026 ;3022:245-257
