Abstract
The crystal structure of the host–guest peptide, (Pro–Pro–Gly)~4~–(Pro–alloHyp–Gly)–(Pro–Pro–Gly)~4~, was analyzed at high resolution. allohydroxyproline (alloHyp), 4S‐hydroxyproline, was successfully characterized through the use of a host–guest peptide, while the previous study indicated the inability of a triple helical formation of (Pro–alloHyp–Gly)~10~. A detailed analysis of alloHyp conformation in collagen‐like models sheds light on the role played by its puckering in the triple‐helix stabilization and destabilization. That is, the alloHyp typically adopts down puckering. However, it adopted up puckering in the Y position in the Pro–alloHyp–Gly guest triplet, which was not preferable conformation for alloHyp. Therefore, the energetically unfavorable conformations seemed to play the key role in giving destabilization to the triple helix in (Pro–alloHyp–Gly)~10~. The intrinsic hydration pattern in (Pro–Pro–Gly)~9~ was conserved even in the surrounding alloHyp residues. © 2005 Wiley Periodicals, Inc. Biopolymers 81: 225–233, 2006
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