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A Biomolecule As A Light Switch

Date:
September 30, 2005
Source:
Max Planck Society
Summary:
Researchers at the Max Planck Institute for Biophysical Chemistry in Goettingen, Germany have uncovered the molecular mechanism of switchable fluorescent proteins, able to switch themselves reversibly back-and-forth between an "on" and "off" state. The discovery could be of importance for, among other purposes, optical data storage in protein crystals.

Snakelocks Anemone (Anemonia sulcata).
Credit: Image : Richard Lockett

Switchable fluorescent proteins - able to switch themselves reversibly back-and-forth between an "on" and "off" state - have been known for only a few years. However, they already hold promise for a large number of novel applications, from cellular biology to data storage. Cell biologists, X-Ray crystallographers, photobiophysicists, and computer-biophysicists from Goettingen have worked together on a project uncovering the molecular mechanism by which a fluorescent protein becomes switched (PNAS, September 13, 2005). This knowledge could be of importance for, among other purposes, optical data storage in protein crystals.


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The above story is based on materials provided by Max Planck Society. Note: Materials may be edited for content and length.


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Max Planck Society. "A Biomolecule As A Light Switch." ScienceDaily. ScienceDaily, 30 September 2005. <www.sciencedaily.com/releases/2005/09/050930083711.htm>.
Max Planck Society. (2005, September 30). A Biomolecule As A Light Switch. ScienceDaily. Retrieved April 23, 2014 from www.sciencedaily.com/releases/2005/09/050930083711.htm
Max Planck Society. "A Biomolecule As A Light Switch." ScienceDaily. www.sciencedaily.com/releases/2005/09/050930083711.htm (accessed April 23, 2014).

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