Mechanism of collagen folding propagation studied by Molecular Dynamics simulations.

ABSTRACT: Collagen forms a characteristic triple helical structure and plays a central role for stabilizing the extra-cellular matrix. After a C-terminal nucleus formation folding proceeds to form long triple-helical fibers. The molecular details of triple helix folding process is of central importance for an understanding of several human diseases associated with misfolded or unstable collagen fibrils. However, the folding propagation is too rapid to be studied by experimental high resolution techniques. We employed multiple Molecular Dynamics simulations starting from unfolded peptides with an already formed nucleus to successfully follow the folding propagation in atomic detail. The triple helix folding was found to propagate involving first two chains forming a short transient template. Secondly

SUBMITTER: Hartmann J 

PROVIDER: S-EPMC8224937 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature