Bondon A, Mouro C
LCOB, UMR CNRS 6509, Université de Rennes 1, Campus de Beaulieu, Rennes Cedex, 35042, France.
J Magn Reson. 1998 Sep;134(1):154-7. doi: 10.1006/jmre.1998.1523.
A new method for NMR spectra acquisition of paramagnetic proteins is described, based on the simple use of homonuclear broadband decoupling of the diamagnetic region. Several advantages are associated with this method which was applied to one-dimensional spectra, to 1D NOE-difference spectroscopy, and to 2D NOESY. The main advantage is a very flat baseline obtained using the PASE (paramagnetic signals enhancement) method. Furthermore, the bulky region of the diamagnetic protons being suppressed, clean NOE-difference spectra can be acquired as well as improved 2D NOESY maps. Applications on 1D 1H spectrum of bovine liver catalase (MW 230,000), and 1D and 2D on the high-spin form of the myoglobin, used as a model protein, are presented.
本文描述了一种用于顺磁蛋白核磁共振谱采集的新方法，该方法基于对抗磁区域的同核宽带去耦的简单应用。此方法应用于一维谱、一维NOE差谱和二维NOESY谱时具有几个优点。主要优点是使用PASE（顺磁信号增强）方法可获得非常平坦的基线。此外，由于抗磁质子的庞大区域被抑制，因此可以采集到清晰的NOE差谱以及改进的二维NOESY图谱。本文展示了该方法在牛肝过氧化氢酶（分子量230,000）的一维氢谱以及用作模型蛋白的高自旋形式肌红蛋白的一维和二维谱上的应用。
