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The path to a folded protein, long a subject of debate, appears in many cases to be long and winding

PHILADELPHIA Its a long-simmering debate in the world of physical chemistry: Does the folding of proteins into biologically active shapes better resemble a luge run fast, linear and predictable or the more freeform trajectories of a ski slope? New research from the University of Pennsylvania offers the strongest evidence yet that proteins shimmy into their characteristic shapes not via a single, unyielding route but by paths as individualistic as those followed by skiers coursing from a mountain summit down to the base lodge.

The new support for a more heterogeneous model of protein folding comes in a paper published today on the Web site of the Proceedings of the National Academy of Sciences.

"The traditional view has been that a protein passes through a series of fixed reactions to reach its folded state," said senior author Feng Gai, a Penn chemist. "Our work suggests quite strongly that folding is a far richer phenomenon. Like skiers, some proteins rocket down an energy gradient to their destination while others take their time, meandering indiscriminately."

Though a fleeting phenomenon, the folding of gangly proteins into tight three-dimensional shapes has broad implications for the growing group of human diseases believed to result from misfolded proteins, most notably neurodegenerative disorders such as Alzheimers and Parkinsons diseases. The characteristic plaques that cripple the brains of Alzheimers and Parkinsons patients are believed to be the dumping grounds for aberrant proteins.

Gais work subtly shifts scientists understanding of one possible remedy: molecular chaperones, promising compounds that "rescue" misfolded proteins and are believed capable of blocking the progression of neurodegenerative disease. Rather than giving sluggish proteins the oomph to finish folding, the Penn work indicates that chaperones may return misfolded proteins to an unfolded state so they can start all over again.

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Contact: Steve Bradt
bradt@pobox.upenn.edu
215-573-6604
University of Pennsylvania
26-Feb-2002


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