Structural and dynamic studies of the gamma-M4 trans-membrane domain of the nicotinic acetylcholine receptor
Structural and dynamic studies of the gamma-M4 trans-membrane domain of the nicotinic acetylcholine receptor
A structural characterization of a synthetic peptide corresponding to the fourth transmembrane domain (M4-TMD) of the ?-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 ?-helical conformation with the helix aligned within 15° 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.
nicotinic acetylcholine receptor, magnetically aligned phases, ether-linked bicelles, cross-polarization magic-angle spinning solid-state nmr
485-496
Williamson, P.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Zandomeneghi, G.
46f1876a-5db6-41f3-88eb-13a5416d38ea
Barrantes, F.J.
495860e8-4b61-408e-8bd3-c3a103df277c
Watts, A.
9d52521b-918a-4f29-aaa7-c2c3f386696f
Meier, B.H.
09278221-d423-4544-95fb-f12bd06201b0
2005
Williamson, P.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Zandomeneghi, G.
46f1876a-5db6-41f3-88eb-13a5416d38ea
Barrantes, F.J.
495860e8-4b61-408e-8bd3-c3a103df277c
Watts, A.
9d52521b-918a-4f29-aaa7-c2c3f386696f
Meier, B.H.
09278221-d423-4544-95fb-f12bd06201b0
Williamson, P.T.F., Zandomeneghi, G., Barrantes, F.J., Watts, A. and Meier, B.H.
(2005)
Structural and dynamic studies of the gamma-M4 trans-membrane domain of the nicotinic acetylcholine receptor.
Molecular Membrane Biology, 22 (6), .
(doi:10.1080/09687860500370653).
Abstract
A structural characterization of a synthetic peptide corresponding to the fourth transmembrane domain (M4-TMD) of the ?-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 ?-helical conformation with the helix aligned within 15° 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.
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Published date: 2005
Keywords:
nicotinic acetylcholine receptor, magnetically aligned phases, ether-linked bicelles, cross-polarization magic-angle spinning solid-state nmr
Identifiers
Local EPrints ID: 45403
URI: http://eprints.soton.ac.uk/id/eprint/45403
ISSN: 0968-7688
PURE UUID: 50e76b02-dc05-4b3e-9e22-d960afcb8321
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Date deposited: 27 Mar 2007
Last modified: 16 Mar 2024 03:53
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Contributors
Author:
G. Zandomeneghi
Author:
F.J. Barrantes
Author:
A. Watts
Author:
B.H. Meier
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