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Scientists post lower speed limit for cell-signaling protein assembly
Date:7/29/2010

or proteins as they spontaneously assemble into their lowest-energy, so-called natural state like a relaxed spring.

"In order to measure how quickly this random, unfolded state changes confirmations, we had to design an entirely new apparatus as well as design and fabricate a microfluidic chip capable of observing proteins within a fraction of a millisecond after being allowed to refold," Waldauer explained. Two lasers were employed to observe the formation of the immunoglobulin proteins.

"We found that the nature of the unfolded state is far from intuitive and that a protein will change from one random conformation to another much more slowly than previously thought," he said.

Scientists know that errors can occur in folding, and these are associated with a variety of diseases including Alzheimer's, ALS, cystic fibrosis and diabetes. Lapidus and colleagues speculate that the rate of the process could influence the outcome. Proteins that wiggle more rapidly, for example, may be more prone to sticking together and causing plaques such as those in Alzheimer's. The team's discovery may lead to new therapeutic strategies for this class of diseases.

"I believe this measurement of intramolecular diffusion is something that will be crucial for any subsequent studies of protein folding or mis-folding," Lapidus said.


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Contact: Mark Fellows
mark.fellows@ur.msu.edu
517-884-0166
Michigan State University
Source:Eurekalert  

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