José N. Onuchic

TL;DR: The work unifies several previously proposed ideas concerning the mechanism protein folding and delimits the regions of validity of these ideas under different thermodynamic conditions.

TL;DR: The energy landscape theory of protein folding suggests that the most realistic model of a protein is a minimally frustrated heteropolymer with a rugged funnel-like landscape biased toward the native structure.

TL;DR: The findings suggest that contacts predicted by DCA can be used as a reliable guide to facilitate computational predictions of alternative protein conformations, protein complex formation, and even the de novo prediction of protein domain structures, contingent on the existence of a large number of homologous sequences which are being rapidly made available due to advances in genome sequencing.

TL;DR: This work states that proteins have a rugged funnel-like landscape biased toward the native structure as a result of evolution, and connecting theory and simulations of minimalist models with experiments has completely revolutionized the understanding of the underlying mechanisms that control protein folding.

TL;DR: In this article, the authors investigated the role of topology in the transition state ensembles of small globular proteins and showed that topology plays a central role in determining the folding mechanism.