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 contg. both chains of (Pro-Pro-Gly)10 and (Pro-Hyp-Gly)10. Results are discussed in relation to the various triple-helix stabilization mechanisms.

Characterization of collagen-like heterotrimers: implications for triple-helix stability.

Berisio Rita;Vitagliano Luigi;
2004

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 contg. both chains of (Pro-Pro-Gly)10 and (Pro-Hyp-Gly)10. Results are discussed in relation to the various triple-helix stabilization mechanisms.
2004
Istituto di Biostrutture e Bioimmagini - IBB - Sede Napoli
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/162682
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