Proline provides site-specific flexibility for in vivo collagen.

ABSTRACT: Fibrillar collagens have mechanical and biological roles, providing tissues with both tensile strength and cell binding sites which allow molecular interactions with cell-surface receptors such as integrins. A key question is: how do collagens allow tissue flexibility whilst maintaining well-defined ligand binding sites? Here we show that proline residues in collagen glycine-proline-hydroxyproline (Gly-Pro-Hyp) triplets provide local conformational flexibility, which in turn confers well-defined, low energy molecular compression-extension and bending, by employing two-dimensional ¹³C-¹³C correlation NMR spectroscopy on ¹³C-labelled intact ex vivo bone and in vitro osteoblast extracellular matrix. We also find that the positions of Gly-Pro-Hyp triplets are h

SUBMITTER: Chow WY 

PROVIDER: S-EPMC6138679 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature