ETH Zürich , Physical Chemistry, Vladimir-Prelog-Weg 2, 8093 Zürich, Switzerland.
Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon , 7 passage du Vercors, 69367 Lyon, France.
J Phys Chem B. 2017 Aug 17;121(32):7671-7680. doi: 10.1021/acs.jpcb.7b06944. Epub 2017 Aug 8.
The structural and dynamical characterization of membrane proteins in a lipid bilayer at physiological pH and temperature and free of crystal constraints is crucial for the elucidation of a structure/dynamics-activity relationship. Toward this aim, we explore here the properties of the outer-membrane protein OmpX embedded in lipid bilayer nanodiscs using proton-detected magic angle spinning (MAS) solid-state NMR at 60 and 110 kHz. [H,N]-correlation spectra overlay well with the corresponding solution-state NMR spectra. Line widths as well as line intensities in solid and solution both depend critically on the sample temperature and, in particular, on the crossing of the lipid phase transition temperature. MAS (110 kHz) experiments yield well-resolved NMR spectra also for fully protonated OmpX and both below and above the lipid phase transition temperature.
在生理 pH 值和温度条件下，并在不受晶体限制的情况下，对脂质双层中的膜蛋白进行结构和动力学表征，对于阐明结构/动力学-活性关系至关重要。为此，我们使用质子探测魔角旋转（MAS）固态 NMR 在 60 和 110 kHz 下研究了嵌入脂质双层纳米盘的外膜蛋白 OmpX 的性质。[H,N]-相关谱与相应的溶液态 NMR 谱吻合得很好。固态和溶液中的线宽和线强度都强烈依赖于样品温度，特别是依赖于脂质相转变温度的交叉。MAS（110 kHz）实验还为完全质子化的 OmpX 以及低于和高于脂质相转变温度的样品产生了分辨率良好的 NMR 谱。
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