Bansal, M and Ramakrishnan, C and Ramachandran, GN (1975) A triple-helical model for (Gly-Pro-Hyp)n with cis peptide units. In: Biopolymers, 14 (12). pp. 2457-2466.
Synthetic regular polytripeptides of the type (Gly-R2-R3) where R2, R3, or both, are imino acids have been widely studied as model compounds for collagen. One such polytripeptide is poly(Gly-Pro-Hyp), since triplets with this sequence constitute about 10% of collagen. Recently, a new model has been proposed for this polytripeptide in which one of the three peptide bonds in the tripeptide unit is in the cis conformation, and the -hydroxyl group of hydroxyproline forms a direct interchain hydrogen bond within the triple helix. We have confirmed this structure by model building using computer techniques, and the helical parameters obtained by us are close to the experimentally observed values. The model is also found to be comparable in stability with other models from energy considerations.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to John Wiley & Sons, Inc.|
|Keywords:||triple helical model;cis peptide;Gly Pro Hyp;polytripeptides|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||08 Jun 2004|
|Last Modified:||19 Sep 2010 04:12|
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