Volume 2, Number 3/4, p.98-100
Ariel Fernández 1,2and María de las Mercedes Boland 3.
What is inherently wrong with the prion structure?
Most soluble proteins thoroughly wrap the amide-carbonyl backbone hydrogen bonds of the native structure by clustering hydrophobic groups around them. In this way, the surrounding water is structured, immobilized or removed, and as a result the backbone hydrogen bonds are stabilized relative to the unbound state. However, we have found an important exception to this trait: the cellular prion proteins, which are by far the worst wrappers of backbone hydrogen bonds among all soluble proteins. This observation helps us understand the structural ambiguity of prions.
Keywords: backbone desolvation, hydrogen bond, prions, protein structure.