PT  - JOURNAL ARTICLE
AU  - Lindorff-Larsen, Kresten
AU  - Piana, Stefano
AU  - Dror, Ron O.
AU  - Shaw, David E.
TI  - How Fast-Folding Proteins Fold
AID  - 10.1126/science.1208351
DP  - 2011 Oct 28
TA  - Science
PG  - 517--520
VI  - 334
IP  - 6055
4099  - http://science.sciencemag.org/content/334/6055/517.short
4100  - http://science.sciencemag.org/content/334/6055/517.full
SO  - Science2011 Oct 28; 334
AB  - An outstanding challenge in the field of molecular biology has been to understand the process by which proteins fold into their characteristic three-dimensional structures. Here, we report the results of atomic-level molecular dynamics simulations, over periods ranging between 100 μs and 1 ms, that reveal a set of common principles underlying the folding of 12 structurally diverse proteins. In simulations conducted with a single physics-based energy function, the proteins, representing all three major structural classes, spontaneously and repeatedly fold to their experimentally determined native structures. Early in the folding process, the protein backbone adopts a nativelike topology while certain secondary structure elements and a small number of nonlocal contacts form. In most cases, folding follows a single dominant route in which elements of the native structure appear in an order highly correlated with their propensity to form in the unfolded state.