Probing the dynamics of a protein hydrophobic core by deuteron solid-state nuclear magnetic resonance spectroscopy.

@article{Vugmeyster2009ProbingTD,
  title={Probing the dynamics of a protein hydrophobic core by deuteron solid-state nuclear magnetic resonance spectroscopy.},
  author={Liliya Vugmeyster and Dmitry M. Ostrovsky and Joseph J Ford and Sarah D. Burton and Andrew S Lipton and Gina L Hoatson and Robert L. Vold},
  journal={Journal of the American Chemical Society},
  year={2009},
  volume={131 38},
  pages={13651-8}
}
With the goal of investigating dynamical features of hydrophobic cores of proteins over a wide range of temperatures, the chicken villin headpiece subdomain protein (HP36) was labeled at a "single" site corresponding to any one of the two C(delta)D(3) groups of leucine-69, which is located in a key position of the core. The main techniques employed are deuteron NMR quadrupolar echo line shape analysis, and T(1Z) (Zeeman) and T(1Q) (quadrupolar order) relaxation experiments performed at 11.7 and… CONTINUE READING