Collagen triple helix molecular structure

Computational studies starting with collagen triple-helix structures now available in the Protein Data Bank are becoming increasingly important for collagen. As described above, molecular dynamics simulations can suggest models that are amenable to experimental verification. Computational analyses and molecular dynamics studies have also been carried out on Gly substitutions in the triple helix (see Section VIII below). 

Brodsky B, Persikov AV. Molecular structure of the collagen triple helix. Adv. Protein Chem. 2005 70 301-339. 

The unique Hyp residue may be important both at the molecular and higher-order structure levels in collagen. Bacteria and viruses lack prolyl hydroxylase and have no hydroxyproline in their collagen-like domains. The significant differences in their amino acid composition and sequence compared to animal collagens suggest the use of alternative stabilization strategies for the triple helix (Rasmussen et al., 2003). 

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