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Protein 'nanosprings' most resilient found in nature

ein structures, characterized by a single, spiral chain of amino acids stabilized by hydrogen bonds.

"We live in a world of forces," Bennett continued. "For example, every time a neuron pushes its way through body tissues to its target, every time a heart beats, or a bicep muscle contracts, forces are generated. Cells have to recognize those forces and adjust accordingly."

The tension created by the ankyrin springs could allow for very rapid translation of mechanical forces into biochemical signals, he said.

The proteins' spring-like properties could also be important for furthering the development of nanotechnology, Marszalek added.

"These nanosprings could provide a wonderful material anytime you need to provide elasticity or force," Marszalek said. "They could open gates, for example, or could perhaps act as shock absorbers in nanomachines of the future."

The researchers plan further work to understand what makes the structure of ankyrin repeats so special and to demonstrate the functional role of this structure to particular ankyrin proteins, such as those involved in hearing, the researchers said. The team will also investigate whether longer springs would maintain the same elastic properties, a finding with important implications for including such proteins in nanodevices.


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Source:Duke University


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