Confinement-induced states in the folding landscape of the Trp-cage miniprotein.

@article{Marino2012ConfinementinducedSI,
  title={Confinement-induced states in the folding landscape of the Trp-cage miniprotein.},
  author={Kristen A. Marino and Peter G. Bolhuis},
  journal={The journal of physical chemistry. B},
  year={2012},
  volume={116 39},
  pages={11872-80}
}
Although protein folding is typically studied in dilute solution, folding in a cell will be affected by interactions with other biomolecules and excluded volume effects. Here, we examine the effect of hydrophobic confinement on folding of the Trp-cage miniprotein. We used replica exchange molecular dynamics simulations to probe the differences between folding in the bulk, on a hydrophobic surface, and confined between two hydrophobic walls. In addition to promotion of helix formation due to… CONTINUE READING

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