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'Disordered' amino acids may really be there to provide wiggle room for signaling protein
Date:5/26/2009

resonance spectroscopy, which can determine a protein's shape by measuring how the individual atomic nuclei of a protein interact with an intense magnetic field.

Since NMR spectroscopy works best with small proteins not large flexible molecules like NHREF1 Roder, his staff scientist Hong Cheng, Ph.D., and their colleagues came up with an innovative technique that allowed them to look at the protein from numerous angles with the NMR spectrometer, and subtract out the overlapping areas to form a more complete picture of the molecule. This picture enabled them to see what NHREF1 looks like in both its "on" and "off" conformation.

"When it is not working, the protein is in this 'off' conformation until acted upon by outside agents" Roder says. "It is a way for the cell to shut off a signaling pathway when it is not in use."

According to Roder, these findings may provide researchers a new way of looking at proteins like NHERF1 and their physiological role in cells.


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Contact: Greg Lester
gregory.lester@fccc.edu
215-728-2753
Fox Chase Cancer Center
Source:Eurekalert

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