Markus M A
Committee on Higher Degrees in Biophysics, Harvard University, Boston, MA 02115, USA.
Pharm Acta Helv. 1996 Jun;71(1):65-78. doi: 10.1016/0031-6865(95)00054-2.
To understand how a protein functions, it is essential to know the three-dimensional structure of the protein to atomic resolution. Multidimensional nuclear magnetic resonance (NMR) techniques provide one method for solving atomic resolution protein structures. These techniques have been applied to the 126-residue protein domain, villin 14T. The most challenging step is assigning each resonance line in the NMR spectrum to the correct proton within the protein. For villin 14T, this sequential assignment step was accomplished with triple-resonance, backbone-directed strategies. The structure reveals a unique fold shared only by domains from other proteins in the actin-severing family.
为了了解蛋白质的功能，至关重要的是要知道蛋白质的三维结构，达到原子分辨率。多维核磁共振（NMR）技术提供了一种解析蛋白质原子分辨率结构的方法。这些技术已应用于由126个残基组成的蛋白质结构域，即绒毛蛋白14T。最具挑战性的步骤是将NMR谱中的每条共振线与蛋白质内正确的质子对应起来。对于绒毛蛋白14T，这一序列归属步骤是通过三共振、基于主链的策略完成的。该结构揭示了一种独特的折叠方式，这种方式仅与肌动蛋白切割家族中其他蛋白质的结构域所共有。
