Picture of UK Houses of Parliament

Leading national thinking on politics, government & public policy through Open Access research

Strathprints makes available scholarly Open Access content by researchers in the School of Government & Public Policy, based within the Faculty of Humanities & Social Sciences.

Research here is 1st in Scotland for research intensity and spans a wide range of domains. The Department of Politics demonstrates expertise in understanding parties, elections and public opinion, with additional emphases on political economy, institutions and international relations. This international angle is reflected in the European Policies Research Centre (EPRC) which conducts comparative research on public policy. Meanwhile, the Centre for Energy Policy provides independent expertise on energy, working across multidisciplinary groups to shape policy for a low carbon economy.

Explore the Open Access research of the School of Government & Public Policy. Or explore all of Strathclyde's Open Access research...

Self-assembly of collagen molecules into fibrils in solution

McCluskey, Andrew and Sindt, Julien and Young, Andrew and Sommerdijk, Nico A.J.M. and Murray, Paul and Camp, Philip J. and Nudelman, Fabio (2016) Self-assembly of collagen molecules into fibrils in solution. In: Gordon Conference on Biomineralisation, 2016-08-14 - 2016-10-19.

[img]
Preview
Text (McCluskey-etal-GCB-2016-Self-assembly-of-collagen-molecules-into-fibrils-in-solution)
McCluskey_etal_GCB_2016_Self_assembly_of_collagen_molecules_into_fibrils_in_solution.pdf
Final Published Version

Download (3MB)| Preview

    Abstract

    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.