A hydrophilic region encompassing 334 amino acids from human type III collagen was produced in Physcomitrella bioreactors and analyzed with respect to prolyl-hydroxylation.
To evaluate the effects of cyclophilin B deficiency on expression levels of collagen family members in dentin, we performed protein identification of cyclophilin B-WT, -Het, and -KO teeth after trypsin digestion.
Collagen has a triple helix form, structured by a [-Gly-Xaa-Yaa-] repetition, where Xaa and Yaa are amino acids. This repeating unit can be post-translationally modified by enzymes, where proline is often hydroxylated into hydroxyproline (Hyp). Two Hyp isomers occur in collagen: 4-hydroxyproline (4H...
