How nature "designs" elastic polymers

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• Dr Jane Clarke, Department of Chemistry
• Thursday 16 November 2006, 16:45-17:15
• Kaetsu Centre, New Hall.

If you have a question about this talk, please contact Duncan Simpson.

The Structure of Living Matter

Many proteins in the body experience and transduce mechanical forces, including proteins in muscle, the extracellular matrix, cell adhesion molecules and proteins in the cytoskeleton. These proteins have to maintain their structure intact when force is applied. This is a protein folding problem – how do proteins resist this force? We are using atomic force microscopy, combined with protein engineering and molecular dynamics simulations to investigate the molecular basis for mechanical strength in elastic proteins. Most elastic proteins are long, with tandem repeats of structurally identical domains, each around 100 amino acids long. Proteins will aggregate (particularly when unfolded) when placed at high concentrations yet in tandem repeat proteins the local concentration of proteins domains is high. There is evidence to suggest that proteins have specific evolved mechanisms to avoid this problem.

This talk is part of the Physics of Living Matter PLM6 series.

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