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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 ...
In protein, hydroxyproline is incorporated into protein by hydroxylation of proline. Pipecolic acid, a heavier analog of proline, is found in efrapeptin. Sarcosine is a N-methylized glycine so its methyl group is used in many biochemical reactions. Azetidine-2-carboxylic acid, which is a smaller homolog of proline in plants.
Proline-rich proteins (PRPs) are a class of intrinsically disordered proteins [1] (IDPs) containing several repeats of a short proline-rich sequence. Many tannin-consuming animals secrete a tannin-binding protein in their saliva. Tannin-binding capacity of salivary mucin is directly related to its proline content.
proline. Secondary amino acids, amino acids containing a secondary amine group are sometimes named imino acids, [2] [3] though this usage is obsolescent. [1] The only proteinogenic amino acid of this type is proline, although the related non-proteinogenic amino acids hydroxyproline [4] [5] [6] and pipecolic acid [7] have often been included in studies of this class of compounds.
Proline-rich protein 21 (PRR21) is a protein of the family of proline-rich proteins. It is encoded by the PRR21 gene, which is found on human chromosome 2, band 2q37.3. [2] The gene exists in several species, both vertebrates and invertebrates, including humans. [3] However, the protein have few conserved regions among species.
Hydroxyproline is found in few proteins other than collagen. For this reason, hydroxyproline content has been used as an indicator to determine collagen and/or gelatin amount. However, the mammalian proteins elastin and argonaute 2 have collagen-like domains in which hydroxyproline is formed.
A new report by the Clean Label Project has found that protein powders may contain something other than muscle-building nutrients: lead and cadmium, both of which are toxic.. The national ...
The thermal stabilization is also hindered when the hydroxyl group has the wrong configuration. Due to the high abundance of glycine and proline contents, collagen fails to form a regular α-helix and β-sheet structure. Three left-handed helical strands twist to form a right-handed triple helix. [5] A collagen triple helix has 3.3 residues per ...