Abstract
The crystal structure of the collagen-based peptide (Pro-Hyp-Gly)4-Pro-Hyp-AIa-(Pro-Hyp-Gly)5 has provided for the first time a highly detailed picture of the architectural elements that come into play in the collagen triple helix. The center of the molecule, which harbors a Gly → Ala substitution, shows subtle conformational changes that result in a local untwisting of the triple helix. The characteristic hydrogen bonding pattern of collagen triple helices is replaced by interstitial water bridges. These effects may be relevant to the diseased states derived from Gly → X mutations in collagens. The possible implications of this disrupted architecture for collagen assemblies are discussed.