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Mechanism Of Protein Folding Unraveled, With Eventual Implications For Treating,,Diseases Caused By Folding Errors

The process of how a protein changes from an initially shapeless string of amino acids to a three-dimensional structure with nooks and crannies of biologically active sites is often called the second half of the genetic code. This transformation is called protein folding.

Research at the University of Pennsylvania Medical Center has recently added some revealing clues as to how this conversion is managed and corrects some misconceptions about how rapidly folding occurs. This active area of research has taken on even more importance with the growing knowledge that errors in protein folding can lead to such deadly and debilitating disorders as Alzheimer's disease, Huntington's-related diseases, and prion-related encephalopathies. A report on this study appears in today's issue of Nature Structural Biology.

How a protein manages to fold is a seemingly impossible problem, suggests S. Walter Englander, PhD, a professor of biochemistry and biophysics at the University of Pennsylvania School of Medicine: "Even with a small, 100-amino-acid-long protein, the number of possible three-dimensional structures that the protein might manifest is larger than the number of molecules in the universe." Protein biologists believe that the amino-acid sequences laid out by the genetic machinery contain chemical instructions for the pathway that carries each protein to its final structure.

The Penn experiments show that the amino-acid chain progresses through a series of pre-determined, intermediate arrangements. Englander's lab has demonstrated that the protein cytochrome c builds its structure in steps by first making helices at either end that lay at right angles to each other. Then, strands, loops, and other helices build up against that initial foundation until the final arrangement is reached. All this can occur in less than one second, but trouble can arise along the way. "A few years ago we showed that on the complicated journey to their fina
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Contact: Karen Young Kreeger
kreeger@mail.med.upenn.edu
215-614-0290
University of Pennsylvania School of Medicine
1-Oct-1998


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