Landon C, Berthault P, Vovelle F, Desvaux H
Centre de Biophysique Moléculaire, CNRS, 45071 Orléans cedex 02, France.
Protein Sci. 2001 Apr;10(4):762-70. doi: 10.1110/ps.47001.
Nonspecific lipid transfer protein from wheat is studied by liquid-state NMR in the presence of xenon. The gas-protein interaction is indicated by the dependence of the protein proton chemical shifts on the xenon pressure and formally confirmed by the first observation of magnetization transfer from laser-polarized xenon to the protein protons. Twenty-six heteronuclear nOes have allowed the characterization of four interaction sites inside the wheat ns-LTP cavity. Their locations are in agreement with the variations of the chemical shifts under xenon pressure and with solvation simulations. The richness of the information obtained by the noble gas with a nuclear polarization multiplied by approximately 12,000 makes this approach based on dipolar cross-relaxation with laser-polarized xenon promising for probing protein hydrophobic pockets at ambient pressure.
利用液态核磁共振技术，在氙气存在的条件下对来自小麦的非特异性脂质转移蛋白进行了研究。蛋白质质子化学位移对氙气压力的依赖性表明了气体与蛋白质之间的相互作用，并且通过首次观察到激光极化氙气到蛋白质质子的磁化转移而得到正式确认。二十六个异核核Overhauser效应（nOes）使得对小麦非特异性脂质转移蛋白（ns-LTP）腔体内四个相互作用位点的特性进行了表征。它们的位置与氙气压力下化学位移的变化以及溶剂化模拟结果一致。通过具有约12,000倍核极化的惰性气体所获得的丰富信息，使得这种基于与激光极化氙气的偶极交叉弛豫的方法有望在常压下探测蛋白质疏水口袋。
