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Hydroxyproline is a major component of the protein collagen, [3] comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [5]
Adams E; Goldstone A (1960). "Hydroxyproline metabolism. III. Enzymatic synthesis of hydroxyproline from Delta1-pyrroline-3-hydroxy-5-carboxylate".
Tissue culture flasks. RPMI 1640, simply known as RPMI medium, is a cell culture medium commonly used to culture mammalian cells. [1] RPMI 1640 was developed by George E. Moore, Robert E. Gerner, and H. Addison Franklin in 1966 at Roswell Park Comprehensive Cancer Center (formerly known as Roswell Park Memorial Institute), from where it derives its name. [2]
Procollagen-proline dioxygenase catalyzes the following reaction: L-proline + alpha-ketoglutaric acid + O 2 → (2S, 4R)-4-hydroxyproline + succinate + CO 2. The mechanism for the reaction is similar to that of other dioxygenases, and occurs in two distinct stages: [3] In the first, a highly reactive Fe(IV)=O species is produced.
In enzymology, a 4-hydroxyproline epimerase (EC 5.1.1.8) is an enzyme that catalyzes the chemical reaction. trans-4-hydroxy-L-proline ...
In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.
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