Researchers in the U.K. have created conditions inside a test tube in which human prion protein can flip back and forth between normal forms and abnormal forms associated with neurodegenerative disease. In its normal form, prion protein is rich in α helix motifs, but when it encounters the abnormal form rich in β sheet motifs, the normal form is thought to misfold and take on the abnormal structure. Reporting in this week’s issue of Science, the researchers describe a chemical solution in which human prion proteins can be induced to alternate between the two folding structures. The technique should allow researchers to design better experiments with which to study the pathology of prion diseases as well as the prion's basic biochemistry.—June Kinoshita

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  1. . Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science. 1999 Mar 19;283(5409):1935-7. PubMed.