Solid-state NMR and molecular dynamics simulations reveal the oligomeric ion-channels of TM2-GABA(A) stabilized by intermolecular hydrogen bonding.

@article{Kandasamy2009SolidstateNA,
  title={Solid-state NMR and molecular dynamics simulations reveal the oligomeric ion-channels of TM2-GABA(A) stabilized by intermolecular hydrogen bonding.},
  author={Senthil Kumar Kandasamy and Dong-kuk Lee and Ravi Prakash Nanga and Jiadi Xu and Jos{\'e} Crist{\'o}bal S{\'a}nchez Santos and Ronald G. Larson and Ayyalusamy Ramamoorthy},
  journal={Biochimica et biophysica acta},
  year={2009},
  volume={1788 3},
  pages={
          686-95
        }
}
The second transmembrane (TM2) domain of GABA(A) receptor forms the inner-lining surface of chloride ion-channel and plays important roles in the function of the receptor protein. In this study, we report the first structure of TM2 in lipid bilayers determined using solid-state NMR and MD simulations. The interatomic (13)C-(15)N distances measured from REDOR magic angle spinning experiments on multilamellar vesicles, containing a TM2 peptide site specifically labeled with (13)C' and (15)N… CONTINUE READING
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