Researchers reveal insights into hidden world of prote...( so they simply do not bind well to thei...)

Frydman discovered TRiC in 1992. She determined that it was important for folding some of the essential proteins and had a complex structure, but was stymied in her efforts to unravel its workings because the technology needed to peer into TRiC's inner sanctum did not yet exist.

Recently, she began an interdisciplinary collaboration with Wah Chiu, a professor at Baylor College of Medicine in Houston, Texas, who is also director of the National Center for Macromolecular Imaging, located at Baylor.

Through combining biological experimentation with high-resolution imaging and computational modeling, Frydman and Chiu (the other senior author of the paper in Nature Structural & Molecular Biology) succeeded in uncovering how the lids at either end of the TRiC chaperonin open and close.

"What we found is that this lid opens like the iris of a camera," Frydman said. "Previously, it was thought that the TRiC opens its lid like the flaps on a cardboard box and that the molecular machine didn't really change shape."

The motion of the lids has major implications for what happens inside the molecule.

"What has been so intriguing is that everything is connected," she said. "This is a very large machine and every part of the machine is communicating with the other parts."

Being so interconnected means that when the lids on the TRiC are twisting open and shut like the aperture on a camera, that rotation is transferred into the interior of the chaperonin. That has provided Frydman with important information on how a protein might line up inside the folding apparatus and how it begins to fold up once the lid is shut.

What they are learning has immense promise from the point of view of protein engineering and production, as well as potential for novel therapeutics, Frydman said.

"If one could understand what the
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