Mechanism and kinetics of peptide partitioning into membranes from all-atom simulations of thermostable peptides.

@article{Ulmschneider2010MechanismAK,
  title={Mechanism and kinetics of peptide partitioning into membranes from all-atom simulations of thermostable peptides.},
  author={Martin B Ulmschneider and Jacques P F Doux and J. Antoinette Killian and Jeremy C. Smith and Jakob P Ulmschneider},
  journal={Journal of the American Chemical Society},
  year={2010},
  volume={132 10},
  pages={3452-60}
}
Partitioning properties of transmembrane (TM) polypeptide segments directly determine membrane protein folding, stability, and function, and their understanding is vital for rational design of membrane active peptides. However, direct determination of water-to-bilayer transfer of TM peptides has proved difficult. Experimentally, sufficiently hydrophobic peptides tend to aggregate, while atomistic computer simulations at physiological temperatures cannot yet reach the long time scales required… CONTINUE READING

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