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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, analysis of the motional averaging of anisotropic interactions present in the solid-state NMR spectra of the reconstituted peptide, indicate that the dynamics of the peptide within the bilayer are highly sensitive to the phase adopted by the lipid bilayer, providing an insight into how the interaction of lipids with this domain may play a important role in the modulation of this receptor by its lipid environment.

Original publication

DOI

10.1080/09687860500370653

Type

Journal article

Journal

Mol Membr Biol

Publication Date

11/2005

Volume

22

Pages

485 - 496

Keywords

Animals, Circular Dichroism, Lipid Bilayers, Nuclear Magnetic Resonance, Biomolecular, Peptides, Protein Structure, Secondary, Protein Structure, Tertiary, Receptors, Cholinergic, Torpedo