Effect of Hydration on the Thermal Stability of the Collagen Triple Helical Structure
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概要
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4(R)-Hydroxyproline (HypR) is often found in natural collagen in spite of being a rare amino acid in proteins overall. It has been known that HypR residue contributes to the thermal stability of the collagen triple helical structure. Intensive studies to investigate the stabilizing mechanism of the collagen triple helical structure have been performed by using a series of polytripeptides (X-Y-Gly)10 [X, Y: Pro, HypR, or 4-fluoroproline (fPro)], The thermodynamic parameters determined by DSC analyses of these model peptides indicate that the enthalpy term contributes predominantly to the thermal stability of (Pro-HypR-Gly)10, whereas the entropy term is primarily responsible for the enhanced stabilities of (Pro-fProR-Gly)10 and (fProS-Pro-Gly)10. Based on the comparison of molecular volumes observed in solution with intrinsic ones from the crystal structure, the difference comes from the difference of hydration on these peptides.
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