The water-soluble β-hairpin, namely the C-terminal domain of im-munoglobulin binding protein GB1, is intensely studied to help understand the factors that govern β-sheet folding. In this article, new light is shed by means of advanced molecular dynamics simulations. The authors show that the folding mechanism is a multiscale process where the turn region conformation leads to two different energy pathways that are connected by elongated structures; structures are fully characterized in the article. This perspective is fully consistent with experimental evidence while it redefines the nature of the unfolded state.
展开▼
