Hydrogen Bond Networks and Hydrophobic Effects in the Amyloid β30-35 Chain in Water: A Molecular Dynamics Study.

@article{Jong2017HydrogenBN,
  title={Hydrogen Bond Networks and Hydrophobic Effects in the Amyloid β30-35 Chain in Water: A Molecular Dynamics Study.},
  author={KwangHyok Jong and Luca Grisanti and Ali Hassanali},
  journal={Journal of chemical information and modeling},
  year={2017},
  volume={57 7},
  pages={
          1548-1562
        }
}
We have studied the conformational landscape of the C-terminal fragment of the amyloid protein Aβ30-35 in water using well-tempered metadynamics simulations and found that it resembles an intrinsically disordered protein. The conformational fluctuations of the protein are facilitated by a collective reorganization of both protein and water hydrogen bond networks, combined with electrostatic interactions between termini as well as hydrophobic interactions of the side chains. The stabilization of… CONTINUE READING
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