Simulation of NMR data reveals that proteins' local structures are stabilized by electronic polarization.

@article{Tong2009SimulationON,
  title={Simulation of NMR data reveals that proteins' local structures are stabilized by electronic polarization.},
  author={Yan Tong and Chang G. Ji and Ye Mei and John Zenghui Zhang},
  journal={Journal of the American Chemical Society},
  year={2009},
  volume={131 24},
  pages={8636-41}
}
Molecular dynamics simulations of NMR backbone relaxation order parameters have been carried out to investigate the polarization effect on the protein's local structure and dynamics for five benchmark proteins (bovine pancreatic trypsin inhibitor, immunoglobulin-binding domain (B1) of streptococcal protein G, bovine apo-calbindin D9K, human interleukin-4 R88Q mutant, and hen egg white lysozyme). In order to isolate the polarization effect from other interaction effects, our study employed both… CONTINUE READING

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