Characterization of collagen-like heterotrimers: implications for triple-helix stability.
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.
Berisio
Rita
R
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 6, I-80134 Napoli, Italy.
Granata
Vincenzo
V
Vitagliano
Luigi
L
Zagari
Adriana
A
D000595:Amino Acid Sequence; D003094:Collagen / Q000737:chemistry*; D006358:Hot Temperature; D006909:Hydroxyproline / Q000737:chemistry; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000737:chemistry; D011489:Protein Denaturation; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary
D010455:Peptides; D003094:Collagen; D011392:Proline; D006909:Hydroxyproline