Johansson M U, de Château M, Björck L, Forsén S, Drakenberg T, Wikström M
Department of Physical Chemistry 2, University of Lund, Sweden.
FEBS Lett. 1995 Oct 30;374(2):257-61. doi: 10.1016/0014-5793(95)01121-t.
We present the first study of the secondary structure and global fold of an albumin-binding domain. Our data show that the GA module from protein PAB, an albumin-binding protein from the anaerobic bacterial species Peptostreptococcus magnus, is composed of a left-handed three-helix bundle. The helical regions were identified by sequential and medium range NOEs, values of NH-C alpha H coupling constants, chemical shift indices, and the presence of slowly exchanging amide protons, as determined by NMR spectroscopy. In addition, circular dichroism studies show that the module is remarkably stable with respect to both pH and temperature.
我们展示了对白蛋白结合结构域二级结构和整体折叠的首次研究。我们的数据表明，来自蛋白质PAB的GA模块，PAB是一种来自厌氧细菌大消化链球菌的白蛋白结合蛋白，由一个左手三螺旋束组成。通过序列和中程核Overhauser效应（NOE）、NH-CαH耦合常数的值、化学位移指数以及通过核磁共振光谱法测定的缓慢交换酰胺质子的存在来确定螺旋区域。此外，圆二色性研究表明，该模块在pH值和温度方面都非常稳定。
