Prions infect cells and turn good proteins bad by inducing structural overhaul. How these proteins replicate is not known, but what is it about their structural elements and sizes that make them infectious?
Structure and infectivity of these proteins has been difficult to analyze using conventional methods, because the proteins are sticky and insoluble, says Claudio Soto of the University of Texas Medical Branch in Galveston, who was not an author on the studies featured here. These three Hot Papers each use different techniques to give detailed looks into the size, structure, and infectivity of different prion proteins. Though the papers are quite different from each other, they are "exemplary" in that they offer "new ways of looking at infectivity," says Andy Hill at the University of Melbourne in Australia, who was also not involved in the studies.
In a June 2005 issue of Nature, David Eisenberg and his group ...
