Communications of the ACM
Sorting Out the Structure of a Parkinson’s Protein
A new model of ed the structure of the protein most commonly associated with Parkinson's disease and found that it can take either a floppy or rigid state, suggesting that forcing the protein to switch to the rigid structure could lead to a new way to tre
Credit: Kelvin C. Luk, Ph.D., Perelman School of Medicine, University of Pennsylvania
Massachusetts Institute of Technology (MIT) computational scientists have modeled the structure of the protein most commonly associated with Parkinson's disease and found that it can take either a floppy or rigid state, suggesting that forcing the protein to switch to the rigid structure could lead to a new way to treat the disease.
"If alpha synuclein can really adopt this ordered structure that does not aggregate, you could imagine a drug-design strategy that stabilizes these ordered structures to prevent them from aggregating," says MIT professor Collin Stultz.
The researchers developed a computer-modeling approach to predict what kind of structures the protein might take. The calculations suggest the protein can rapidly switch among many different conformations. At any moment, about 70 percent of individual proteins will be in one of the many possible disordered states, which exist as single molecules. When a few of the proteins join together, they can assume a mix of possible rigid structures.
Some researchers believe the states are disordered, while others say they are ordered, and both are at least partially correct, according to Stultz. "This paper seems to bridge the gap" between the two camps, says University of Kentucky professor Trevor Creamer.
From MIT News
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