Characterization of collagen‐like heterotrimers: Implications for triple‐helix stability
Rita Berisio, Vincenzo Granata, Luigi Vitagliano, Adriana Zagari
Abstract
Rita Berisio, Vincenzo Granata, Luigi Vitagliano, Adriana Zagari
Abstract
This article deals with the effects of proline hydroxylation on collagen triple-helix stability, an issue that is still under discussion. To investigate the structural determinants of triple-helix stabilization by hydroxyproline (Hyp), we here characterized spectroscopically triple-helix heterotrimers containing both chains of (Pro-Pro-Gly)10 and (Pro-Hyp-Gly)10. Results are discussed in relation to the various triple-helix stabilization mechanisms.
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This article deals with the effects of proline hydroxylation on collagen triple-helix stability, an issue that is still under discussion. To investigate the structural determinants of triple-helix stabilization by hydroxyproline (Hyp), we here characterized spectroscopically triple-helix heterotrimers containing both chains of (Pro-Pro-Gly)10 and (Pro-Hyp-Gly)10. Results are discussed in relation to the various triple-helix stabilization mechanisms.
Key concepts: Triple helix, Collagen helix, Chemistry, Hydroxylation, Hydroxyproline, Helix (gastropod), Proline, Stereochemistry