Williamson P T F, Zandomeneghi G, Barrantes F J, Watts A, Meier B H
Physical Chemistry, ETH, Zurich, Switzerland.
Mol Membr Biol. 2005 Nov-Dec;22(6):485-96. doi: 10.1080/09687860500370653.
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.
已对来自加州电鳐的烟碱型乙酰胆碱受体γ亚基的第四个跨膜结构域（M4-TMD）对应的合成肽进行了结构表征。固态核磁共振和圆二色光谱研究表明，在重构到脂质囊泡或磁取向脂质双层中后，合成的M4-TMD采用线性α-螺旋构象，螺旋与膜法线的夹角在15度以内。此外，对重构肽的固态核磁共振谱中存在的各向异性相互作用的运动平均分析表明，肽在双层中的动力学对脂质双层所采用的相高度敏感，这为脂质与该结构域的相互作用如何在其脂质环境对该受体的调节中发挥重要作用提供了见解。
