Researchers observe single protein dimers wavering between two symmetrically opposed structures

Researchers at The Scripps Research Institute, the University of California, San Diego, and Ohio State University have used a very sensitive fluorescence technique to find that a bacterial protein thought to exist in one "natural" three-dimensional structure (shape), can actually twist itself into a second form, depending on the protein's chemical environment. One folded form is active and the other is inactive, but the protein can easily morph from one state to another.

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<p><a href="http://www.physorg.com/news164652632.html">Researchers observe single protein dimers wavering between two symmetrically opposed structures</a></p> <p>Researchers at The Scripps Research Institute, the University of California, San Diego, and Ohio State University have used a very sensitive fluorescence technique to find that a bacterial protein thought to exist in one "natural" three-dimensional structure (shape), can actually twist itself into a second form, depending on the protein's chemical environment. One folded form is active and the other is inactive, but the protein can easily morph from one state to another.</p>