This page has been accessed 155,056 times. The function of collagen is to provide structural support and strength in the skin, bones, and connective tissues. Vitamin C is needed to produce essential amino acids used to make collagen. Bonds are further strengthened thus forming the insoluble collagen fibril [1] [2]. Scurvy is an acquired collagen-associated disease caused by vitamin C deficiency. The sources cited below consist of evidence from peer-reviewed journals, prominent medical organizations, academic associations, and government data. It is one of the most plentiful proteins present in mammals and it is responsible for performing a variety of important biological functions. Her extensive experience as a professional science writer is complemented by her scientific credentials. The helix forms because of the regular amino acid sequence of the strands. Without it, collagen fibers cannot be repaired, and blood vessels, tendons and bones become fragile. It is most well-known for the structural role it plays in the body. Twenty eight different types of collagen have been identified in vertebrates. The triple-helical domain structure of collagens consists of three distinct α-chains and earns collagen the name "tropocollagen" [2]. Start studying Collagen Structure and Function. It is most well-known for the structural role it plays in the body. Copyright © 2020 Leaf Group Ltd., all rights reserved. During the process of collagen synthesis, free-hydroxyproline and hydroxylysine peptides appear as by-products, some of which are metabolized and may appear in urine [1]. Shampoo advertisements have made us aware of collagen as a structural protein found in our hair 2. The shape and structural properties of a native collagen molecule are established by its triple-helical α-domain(s). There are many types of disorders associated with collagen.These disorders typically occur as a result of improper folding of these molecules and occasionally due to a particular amino acid substitution [2]. A number of diseases are associated with collagen abnormalities or damage. Collagen can allow a tissue to withstand immense pulling pressure without stretching -- for example in a tendon transmitting the pull of a muscle to a bone. The unique properties of each type are due to segments in the collagen molecules that disrupt the helical structure. She holds a Bachelor of Arts in natural science from the University of Cambridge UK, and is currently working towards a PhD in infectious disease. Each of these chains contain a characteristic L-handed amino acid sequence of polyproline, often termed as polyproline type II helix [4]. Upon exposure to boiling water, collagen is converted to gelatin. The sequence is a repeating pattern of glycine-proline-X, where X can be any amino acid. The triple helix structure of collagen gives the structure strength and therefore the function of collagen is to provide mechanical strength in many areas. The image on the right-hand side has each side chain colored a different color to shown how each individual jmolSetTarget('1');jmolLink('delete $clickGreenLinkEcho; refresh;setL = \"setLoading();\"; javascript @setL; script /wiki/extensions/Proteopedia/spt/wipeFullLoadButton.spt; isosurface DELETE; scn = load(\"/wiki/scripts/Sandbox_168/Helices/1.spt\"); scn = scn.replace(\'_setSelectionState;\', \'_setSelectionState; message Scene_finished;\'); script inline scn;','helices','helices'); interact with the others to form the overall molecule. Structure of collagen • Amino acid sequence: • Collagen is rich in proline and glycine, both of which are important in the formation of the triple-stranded helix. Collagen forms fibrils that provide the structure for fibrous tissue, such as ligaments, tendons, and skin. It also replaces and restores dead skin cells. 8-10, D-91054 Erlangen, Germany bDepartment of Experimental Medicine I, University of Erlangen-Nu¨rnberg, 91054 Erlangen, Germany Received 20 January 2003; accepted 26 August 2003 It is one of the most plentiful proteins present in mammals and it is responsible for performing a variety of important biological functions. in the Descemet's membrane in the cornea [79] . The structure of tendons can be divided into six major areas. 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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