Ramamoorthy A, Marassi F M, Zasloff M, Opella S J
Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA.
J Biomol NMR. 1995 Nov;6(3):329-34. doi: 10.1007/BF00197814.
A three-dimensional 1H chemical shift/1H-15N dipolar coupling/15N chemical shift correlation spectrum was obtained on a sample of specifically 15N-labeled magainin peptides oriented in lipid bilayers between glass plates in a flat-coil probe. The spectrum showed complete resolution of the resonances from two labeled amide sites in all three dimensions. The three orientationally dependent frequencies associated with each resonance enabled the orientation of the peptide planes to be determined relative to the direction of the applied magnetic field. These results demonstrate the feasibility of multiple-pulse spectroscopy in a flat-coil probe, the ability to measure three spectral parameters from each site in a single experiment, and the potential for resolving among many labeled sites in oriented membrane proteins.
在一个扁平线圈探头中，对置于玻璃板间脂质双层中特定15N标记的蛙皮素肽样品进行了三维1H化学位移/1H-15N偶极耦合/15N化学位移相关谱测定。该谱在所有三个维度上均显示出两个标记酰胺位点共振的完全分辨。与每个共振相关的三个取向相关频率能够确定肽平面相对于外加磁场方向的取向。这些结果证明了在扁平线圈探头中进行多脉冲光谱学的可行性、在单个实验中从每个位点测量三个光谱参数的能力以及在取向膜蛋白中多个标记位点间进行分辨的潜力。
