UCSB physicists have made a device that can make fast molecular measurements, to better understand protein folding. Everett Lipman, assistant professor of physics at UCSB, has stated in a press release that protein “misfolding and aggregation … are thought to cause … diseases such as Alzheimer’s and Parkinson’s.” The announcement indicates that the device may facilitate research for discovering the root of these diseases.
UCSB physicists and the University of Zurich conducted a study (published in this week’s online issue of the Proceedings of the National Academy of Scientists) in which the device was used to make single-molecule measurements of the inside of chaperonin—a molecular “chaperone” which assists the folding of other proteins, while preventing the proteins from clumping together. The team expressed in a press release that they wanted to understand how chaperonin functions and fails to function.
To make the five-milisecond measurements of chaperonin, the team mixed fluids containing chaperonin and proteins in a channel one-tenth the size of human hair. They discovered that chaperonin slows the folding of one portion of the protein so that it finds the correctly folded shape without connecting to anything else. The team hopes to expand this study to conclude whether the failure of chaperonin is responsible for the misfolding and aggregation of proteins which causes diseases such as Alzheimer’s and Parkinson’s.