Native contacts determine protein folding mechanisms in atomistic simulations.

@article{Best2013NativeCD,
  title={Native contacts determine protein folding mechanisms in atomistic simulations.},
  author={Robert B. Best and Gerhard Hummer and William Allen Eaton},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 44},
  pages={
          17874-9
        }
}
The recent availability of long equilibrium simulations of protein folding in atomistic detail for more than 10 proteins allows us to identify the key interactions driving folding. We find that the collective fraction of native amino acid contacts, Q, captures remarkably well the transition states for all the proteins with a folding free energy barrier. Going beyond this global picture, we devise two different measures to quantify the importance of individual interresidue contacts in the… CONTINUE READING

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