Collagen Structure & Function: Difference between revisions
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==Molecular Structure== | ==Molecular Structure== | ||
The shape and structural properties of a native collagen molecule are established by its triple-helical α-domain(s). In classical collagen molecules a single triple-helical domain is observed to compose close to 95% of the molecule <ref>PMID: 19853297</ref>. However there are also other types of collagens that exist which have been shown to comprise of multiple triple-helical α-domains which only account for a fraction of the molecule's overall mass. | The shape and structural properties of a native collagen molecule are established by its triple-helical α-domain(s). In classical collagen molecules a single triple-helical domain is observed to compose close to 95% of the molecule.<ref name="residues">PMID:19853297</ref>. However there are also other types of collagens that exist which have been shown to comprise of multiple triple-helical α-domains which only account for a fraction of the molecule's overall mass. | ||
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have also been illustrated to point out their positions in the triple-helix. | have also been illustrated to point out their positions in the triple-helix. | ||
[[Image:collagen_(alpha_chain).jpg | thumb | Amino Acid residues in collagen. Gly, Pro and Hydroxyproline residues present in a collagen molecule. ]] | [[Image:collagen_(alpha_chain).jpg | thumb | Amino Acid residues in collagen. Gly, Pro and Hydroxyproline residues present in a collagen molecule. ]].<ref name="residues" />. | ||
==Function== | ==Function== | ||