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A polyproline helix is a type of protein secondary structure which occurs in proteins comprising repeating proline residues. [1] A left-handed polyproline II helix (PPII, poly-Pro II, κ-helix [2]) is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly (-75°, 150°) and have trans isomers of their peptide bonds.
Multiple prolines and/or hydroxyprolines in a row can create a polyproline helix, the predominant secondary structure in collagen. The hydroxylation of proline by prolyl hydroxylase (or other additions of electron-withdrawing substituents such as fluorine ) increases the conformational stability of collagen significantly. [ 20 ]
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The collagen triple helix is made of three collagen peptides, each of which forms its own left-handed polyproline helix. [5] When the three chains combine, the triple helix adopts a right-handed orientation. The collagen peptide is composed of repeats of Gly-X-Y, with the second residue (X) usually being Pro and the third (Y) being ...
In addition to the protein domains, there are unusual transmembrane elements formed by peptides. A typical example is gramicidin A, a peptide that forms a dimeric transmembrane β-helix. [8] This peptide is secreted by gram-positive bacteria as an antibiotic. A transmembrane polyproline-II helix has not been reported in natural proteins ...
Perusahaan Perdagangan Indonesia, trading company Philips Phonographische Industries , later Philips Records Phonographic Performance Ireland , music licensing company
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57479 233210 Ensembl ENSG00000126464 ENSMUSG00000046574 UniProt Q9ULL5 E9PYL2 RefSeq (mRNA) NM_020719 NM_175022 RefSeq (protein) NP_065770 NP_778187 Location (UCSC) Chr 19: 49.59 – 49.63 Mb Chr 7: 44.68 – 44.7 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Proline-rich 12 (PRR12) is a protein of unknown function encoded by the gene PRR12. Gene The Homo sapiens PRR12 gene is ...