Type I collagen is a major constituent of many biological tissues, including skin, bone, tendon and cartilages. Its main functions are to shape extracellular matrices, promote cell attachment and provide tissues with strength, flexibility and elasticity. At the core these functions is its remarkable ability of collagen to form highly organized fibrils through the self-assembly of the molecules. The fibrilogenesis involves the lateral association of collagen triple helices into staggered parallel arrays that give rise to the characteristic D-band periodicity of 67 nm. Currently, the mechanisms of collagen self-assembly are poorly understood. Here, we combine the nanometer-scale resolution of cryo-transmission electron microscopy (cryoTEM) with molecular dynamics to investigate the self-assembly of collagen molecules into fibrils in solution.
|Number of pages||1|
|Publication status||Published - 14 Aug 2016|
|Event||Gordon Conference on Biomineralisation - Barcelona, Spain|
Duration: 14 Aug 2016 → 19 Oct 2016
|Conference||Gordon Conference on Biomineralisation|
|Period||14/08/16 → 19/10/16|