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Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [ 5 ] In the canonical collagen Xaa-Yaa-Gly triad (where Xaa and Yaa are any amino acid), a proline occupying the Yaa position is hydroxylated to give a Xaa-Hyp-Gly sequence.
Furthermore, proline is rarely found in α and β structures as it would reduce the stability of such structures, because its side chain α-nitrogen can only form one nitrogen bond. Additionally, proline is the only amino acid that does not form a red-purple colour when developed by spraying with ninhydrin for uses in chromatography. Proline ...
Glycine, proline, and hydroxyproline must be in their designated positions with the correct configuration. For example, hydroxyproline in the Y position increases the thermal stability of the triple helix, but not when it is located in the X position. [4] The thermal stabilization is also hindered when the hydroxyl group has the wrong ...
A number of Wikipedia articles contain pro and con lists: lists of arguments for and against some particular contention or position.These take several forms, including lists of advantages and disadvantages of a technology; pros and cons of a proposal which may be as technical as Wi-Fi or otherwise; and lists of criticisms and defenses of a political position or other view (such as socialism or ...
Procollagen-proline dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as alpha-ketoglutarate-dependent hydroxylases. These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires alpha-Ketoglutaric acid , Fe 2+ , and ascorbate .
Hence, this enzyme has one substrate, trans-4-hydroxy-L-proline, and one product, cis-4-hydroxy-D-proline. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is 4-hydroxyproline 2-epimerase.
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Collagen is a structural protein found i.a. in bone, skin and connective tissues that is broken down into iminodipeptides at the end of its lifecycle. Of these dipeptides, those containing C-terminal proline or hydroxyproline would normally be broken down further by the enzyme Prolidase, recovering and thus recycling the constituent amino acids.