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Updated: Jul 15, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Imino acids and collagen triple helix stability: characterization of collagen-like polypeptides containing
Rita Berisio1, Vincenzo Granata, Luigi Vitagliano
1Istituto di Biostrutture e Bioimmagini, CNR; Dipartimento di Chimica Biologica, Università degli Studi di Napoli Federico II, Centro interuniversitario di ricerca sui Peptidi bioattivi (C.I.R.P.E.B.), Via Mezzocannone 6, I-80134 Naples, Italy.
Abstract:
The analysis of factors contributing to the stability of proteins is a subject of intense debate. Particularly challenging is the study of structural proteins, since their function is their structure. Among these is collagen, the key structural component of bones, skin, cartilage, tendons, and other connecting tissues. It is well established that the collagen triple helix is characterized by the presence of hydroxyproline, whose content modulates triple helix thermal stability according to the requirement of the host organism. Because of the complexity and the fibrous nature of collagen, data on the stability and structure of this protein have been mainly obtained by the use of collagen-like polypeptides. On the basis of CD characterization of collagen-like polypeptides we here show that the presence of Hyp at the X position of repeating triplets Hyp-Hyp-Gly stabilizes the triple helix significantly. This extra-stabilization has been ascribed, by using molecular modeling, to the formation of a hydrogen bond between Hyp residues belonging to the X and the Y positions of adjacent chains. This communication also provides a comprehensive interpretation of the ensemble of available data on polypeptides containing proline derivatives.
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