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In brewing, proteins rich in proline combine with polyphenols to produce haze (turbidity). [25] L-Proline is an osmoprotectant and therefore is used in many pharmaceutical and biotechnological applications. The growth medium used in plant tissue culture may be supplemented with proline. This can increase growth, perhaps because it helps the ...
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.
Chromosome 19 open reading frame 55 (C19orf55), also known as PROSER3 or Proline And Serine-Rich Protein 3, is an uncharacterized human protein-coding gene.PROSER3 (accession: NM_001039887) is found on the plus strand of chromosome 19 at gene locus q.13.12 at the span of 12,991 base pairs, see Figure "Ideogram of chromosome 19 showing PROSER3 in Humans".
The common natural forms of amino acids have a zwitterionic structure, with −NH + 3 (−NH + 2 − in the case of proline) and −CO − 2 functional groups attached to the same C atom, and are thus α-amino acids, and are the only ones found in proteins during translation in the ribosome.
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.
In particular, the L-amino acids normally found in proteins can spontaneously isomerize at the atom to form D-amino acids, which cannot be cleaved by most proteases. Additionally, proline can form stable trans-isomers at the peptide bond.
Plant-based protein powders—made from rice, peas or soy—were found to contain triple the amount of lead compared to whey protein powders, which are made from the liquid byproduct of cheese ...
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.