Altieri Amanda S, Byrd R Andrew
Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, Maryland 21702, USA.
Curr Opin Struct Biol. 2004 Oct;14(5):547-53. doi: 10.1016/j.sbi.2004.09.003.
The automation of protein structure determination using NMR is coming of age. The tedious processes of resonance assignment, followed by assignment of NOE (nuclear Overhauser enhancement) interactions (now intertwined with structure calculation), assembly of input files for structure calculation, intermediate analyses of incorrect assignments and bad input data, and finally structure validation are all being automated with sophisticated software tools. The robustness of the different approaches continues to deal with problems of completeness and uniqueness; nevertheless, the future is very bright for automation of NMR structure generation to approach the levels found in X-ray crystallography. Currently, near completely automated structure determination is possible for small proteins, and the prospect for medium-sized and large proteins is good.
利用核磁共振（NMR）技术进行蛋白质结构测定的自动化正在走向成熟。从繁琐的共振归属过程，接着是核Overhauser效应（NOE）相互作用的归属（现在与结构计算交织在一起），为结构计算组装输入文件，对错误归属和不良输入数据进行中间分析，到最后的结构验证，所有这些都通过复杂的软件工具实现了自动化。不同方法的稳健性仍在继续应对完整性和唯一性的问题；尽管如此，NMR结构生成自动化达到X射线晶体学水平的前景非常光明。目前，对于小蛋白质，几乎完全自动化的结构测定是可行的，对于中等大小和大蛋白质的前景也很好。
