Hydroxylation-induced Stabilization of the Collagen Triple Helix
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
1. Hydroxyproline content and location in relation to collagen thermal stability
2. A Thermodynamic Analysis of the Contribution of Hydroxyproline to the Structural Stability of the Collagen Triple Helix
3. The triple helix ? coil conversion of collagen-like polytripeptides in aqueous and nonaqueous solvents. Comparison of the thermodynamic parameters and the binding of water to (L-Pro-L-Pro-Gly)n and (L-Pro-L-Hyp-Gly)n
4. Structural bases of collagen stabilization induced by proline hydroxylation
5. Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability
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