At least 10% shorter C-H bonds in cryogenic protein crystal structures than in current AMBER forcefields.

@article{Pang2015AtL1,
  title={At least 10% shorter C-H bonds in cryogenic protein crystal structures than in current AMBER forcefields.},
  author={Yanyang Pang},
  journal={Biochemical and biophysical research communications},
  year={2015},
  volume={458 2},
  pages={
          352-5
        }
}
High resolution protein crystal structures resolved with X-ray diffraction data at cryogenic temperature are commonly used as experimental data to refine forcefields and evaluate protein folding simulations. However, it has been unclear hitherto whether the C-H bond lengths in cryogenic protein structures are significantly different from those defined in forcefields to affect protein folding simulations. This article reports the finding that the C-H bonds in high resolution cryogenic protein… CONTINUE READING
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