Structural and dynamic studies of the gamma-M4 trans-membrane domain of the nicotinic acetylcholine receptor.

@article{Williamson2005StructuralAD,
  title={Structural and dynamic studies of the gamma-M4 trans-membrane domain of the nicotinic acetylcholine receptor.},
  author={Philip T F Williamson and Giorgia Zandomeneghi and Francisco J. Barrantes and Anthony Watts and Beat H Meier},
  journal={Molecular membrane biology},
  year={2005},
  volume={22 6},
  pages={
          485-96
        }
}
A structural characterization of a synthetic peptide corresponding to the fourth transmembrane domain (M4-TMD) of the gamma-subunit of the nicotinic acetylcholine receptor from Torpedo californica has been undertaken. Solid-state NMR and CD spectroscopy studies indicate that upon reconstitution into lipid vesicles or magnetically aligned lipid bilayers, the synthetic M4-TMD adopts a linear alpha-helical conformation with the helix aligned within 15 degrees of the membrane normal. Furthermore… CONTINUE READING

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