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Researchers observe single protein dimers wavering between two symmetrically opposed structures
Date:6/19/2009

says.

This suggests that cells could easily regulate how such proteins within them are folded, and thus alter their function.

Theoretically, it would only take different binding partners or changes in the cell's pH, ions, or the presence of other small molecules to regulate how a protein is folded within a cell, he says. "Furthermore, proteins could be folded in one structure in one area of the cell, and configured differently in another location of the same cell depending on whether or not they need to be active."

"Such a powerful mechanism has lots of clinical implications," Deniz says. "Small mutations in proteins could throw off the delicate balance of energy that is needed between conformational structures of proteins in a cell, leading to disease. If so, a drug might be able to reverse those kinds of imbalances."


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Contact: Keith McKeown
kmckeown@scripps.edu
858-784-8134
Scripps Research Institute
Source:Eurekalert

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