Sandbox GGC9: Difference between revisions
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==Crystal Structure of Collagen Adhesin and Collagen Complex== | ==Crystal Structure of Collagen Adhesin and Collagen Complex== | ||
Collagen is one of the most abundance protein in the body. There are thought to be four types of collagen in which give rise to different structures of the body (bones, tendons, cartilage, skin, basement membranes, etc.) The collagenous domains have a characteristic triple helix structure where each of the participating polypeptides are repeating Gly-X-Y sequences that either form heterotrimeric or homotrimetric L-proline helices. | Collagen is one of the most abundance protein in the body. There are thought to be four types of collagen in which give rise to different structures of the body (bones, tendons, cartilage, skin, basement membranes, etc.) The collagenous domains have a characteristic triple helix structure where each of the participating polypeptides are repeating Gly-X-Y sequences that either form heterotrimeric or homotrimetric L-proline helices. | ||
<Structure load=' | <Structure load='2f6a' size='350' frame='true' align='right' caption='Insert caption here' scene='Collagenadhesincomplex/1' /> | ||
Revision as of 02:24, 23 April 2018
Crystal Structure of Collagen Adhesin and Collagen Complex
Collagen is one of the most abundance protein in the body. There are thought to be four types of collagen in which give rise to different structures of the body (bones, tendons, cartilage, skin, basement membranes, etc.) The collagenous domains have a characteristic triple helix structure where each of the participating polypeptides are repeating Gly-X-Y sequences that either form heterotrimeric or homotrimetric L-proline helices.
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Function
Disease
Relevance
Structural highlights
This is the structural resiude of 4-HydroxyprolineCollagen Adhesion and Complex by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
