True about collagen is all Except
COLLAGENS HAVE A TRIPLE HELIX STRUCTUREAll collagen types have a triple helical structure. A striking characteristic of collagen is the occurrence of glycine residues at every third position of the triple helical poion of the alpha chain. This is necessary because glycine is the only amino acid small enough to be accommodated in the limited space available in the central core of the triple helix.This repeating structure, represented as (Gly-X-Y)n, is an absolute requirement for the formation of the triple helix. While X and Y can be any other amino acids, about 100 of the X positions are proline and about 100 of the Y positions are hydroxyproline. Proline and hydroxyproline confer rigidity on the collagen molecule. Hydroxyproline is formed by the post-translational hydroxylation of peptide-bound proline residues catalyzed by the enzyme prolyl hydroxylase, whose cofactors are ascorbic acid (vitamin C) and a-ketoglutarate.Ref: Harper&;s Biochemistry; 30th edition; Chapter 50 The Extracellular Matrix
Triple helix
Beta pleated sheet
Vit C is necessary for post translational modification
Glycine residue at every third position
Structure and function of protein