Protein folding: where is the paradox?

In this contribution we shall try to argue that no folding scenario - be it hierachical, nonhierarchical, nucleation, etc. - needs to be invoked to solve Levinthal's paradox: It fails on its own grounds.

Solvent environment conducive to protein aggregation.

The effect of solvent structuring induced by molecular crowding is elucidated within a competitive situation involving protein folding and aggregation. Two patterned fragments of amyloidogenic proteins are chosen as study cases and analyzed by molecular dynamics with an implicit treatment of the solvent. The extent of crowding needed to induce aggregation is determined.