Abstract
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.
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Science (New York, N.Y.) |
| Vol/bind | 334 |
| Udgave nummer | 6055 |
| Sider (fra-til) | 517-20 |
| Antal sider | 4 |
| DOI | |
| Status | Udgivet - 28 okt. 2011 |
| Udgivet eksternt | Ja |