Final answer:
Three helices of collagen interact to form a right-handed triple helix, providing strength and elasticity to connective tissues due to the stable arrangement of amino acids, particularly proline and hydroxyproline. The triple helix maintains the protein's three-dimensional shape, crucial for its function.
Step-by-step explanation:
When three helices of collagen interact, they form a triple helix, which is a secondary structure found in the collagen protein. Each of the three collagen peptides is a left-handed helix, and when they come together, they form a right-handed triple helix. This structure provides collagen with its unique strength and elasticity, which is essential for the function of connective tissues in the body.
The collagen peptide consists of a repeating sequence of Gly-X-Y, with proline and hydroxyproline being common in the X and Y positions, respectively. These amino acids contribute to the stability and rigidity of the collagen molecule. The hydroxyproline enables more hydrogen bonding, which strengthens the connective tissues further. Synthesis of collagens involves several stages, with proline and lysine undergoing posttranslational modifications, such as hydroxylation, which is assisted by enzymes requiring vitamin C as a cofactor.
All these interactions between amino acids determine the protein's three-dimensional shape, which is critical for its functionality. If the three-dimensional structure is lost, the protein may no longer work as intended, highlighting the importance of the triple helix configuration in maintaining collagen's structural integrity.