VATIS UPDATE Article

Biophysicists at JILA (a joint institute of the University of Colorado and the National Institute of Standards and Technology [NIST], the United States) have measured protein folding in more detail than ever before, revealing behavior that is surprisingly more complex than previously known. The results suggest that, until now, much about protein behavior has been hidden to science – happening on faster timescales and with finer changes in structure than conventional methods could detect.

The JILA research revealed many previously unknown states by unfolding an individual protein. For example, the JILA team identified 14 intermediate states – seven times as many as previously observed – in just one part of bacteriorhodopsin, a protein in microbes that converts light to chemical energy and is widely studied in research. “The increased complexity was stunning. Better instruments revealed all sorts of hidden dynamics that were obscured over the last 17 years when using conventional technology,” said Tom Perkins, at JILA.

Knowledge of protein folding is important because proteins must assume the correct 3-D structure to function properly. Misfolding may inactivate a protein or make it toxic. Several neurodegenerative and other diseases are attributed to incorrect folding of certain proteins. Over the last 50 years, protein folding has become the focus of a large, interdisciplinary research field. Significantly, bacteriorhodopsin is a membrane protein that resides in the boundary between the inside and outside of cells.