Related Experiment Video
Updated: Jan 21, 2026

In Vivo Hydroxyl Radical Protein Footprinting for the Study of Protein Interactions in Caenorhabditis elegans
Published on: April 1, 2020
Role of prolyl hydroxylation in the molecular interactions of collagens
Pekka Rappu1, Antti M Salo2, Johanna Myllyharju2
1Department of Biochemistry, University of Turku, FI-20014, Finland.
Abstract:
Co- and post-translational hydroxylation of proline residues is critical for the stability of the triple helical collagen structure. In this review, we summarise the biology of collagen prolyl 4-hydroxylases and collagen prolyl 3-hydroxylases, the enzymes responsible for proline hydroxylation. Furthermore, we describe the potential roles of hydroxyproline residues in the complex interplay between collagens and other proteins, especially integrin and discoidin domain receptor type cell adhesion receptors. Qualitative and quantitative regulation of collagen hydroxylation may have remarkable effects on the properties of the extracellular matrix and consequently on the cell behaviour.
Related Concept Videos
Molecular and Ionic Solids
Molecular Solids
Molecular crystalline solids, such as ice, sucrose (table sugar), and iodine, are solids that are composed of neutral molecules as their constituent units. These molecules are held together by weak intermolecular forces such as London dispersion forces, dipole-dipole interactions, or hydrogen bonds, which...
Fibril-associated Collagen
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Molecular Orbital Theory I
Molecular Shape and Polarity
Molecular Models
Molecular Chaperones and Protein Folding
The...

