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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]
Dipalmitoylphosphatidylcholine (DPPC) is a phospholipid (and a lecithin) consisting of two C 16 palmitic acid groups attached to a phosphatidylcholine head-group.. It is the main constituent of pulmonary surfactants, which reduces the work of breathing and prevents alveolar collapse during breathing.
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.
1-Oleoyl-2-palmitoyl-phosphatidylcholine. Phosphatidylcholines (PC) are a class of phospholipids that incorporate choline as a headgroup.They are a major component of biological membranes and can easily be obtained from a variety of readily available sources, such as egg yolk or soybeans, from which they are mechanically or chemically extracted using hexane.
In nature, proline, hydroxyproline, pipecolic acid and sarcosine are well-known secondary amino acids. Proline is the only proteinogenic secondary amino acids. Other secondary amino acids are non-proteinogenic amino acids. In protein, hydroxyproline is incorporated into protein by hydroxylation of proline.
Phosphatidylinositol 4,5-bisphosphate or PtdIns(4,5)P 2, also known simply as PIP 2 or PI(4,5)P 2, is a minor phospholipid component of cell membranes. PtdIns(4,5)P 2 is enriched at the plasma membrane where it is a substrate for a number of important signaling proteins. [1]
The structural properties of HypSys, containing hydroxyproline and being glycosylated, indicate that they are synthesised through the secretory system. [2] The precursor to HypSys in tomato is a 146 amino acid polypeptide, exclusively synthesised within the vascular bundles of leaves and petioles associated with parenchyma cells of phloem bundles.
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.
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