Poulsen F M, Hoch J C, Dobson C M
Biochemistry. 1980 Jun 10;19(12):2597-607. doi: 10.1021/bi00553a011.
Saturation of specific proton nuclear magnetic resonance (NMR) signals from residues in the hydrophobic box region of lysozyme (EC 3.2.1.17) has enabled negative nuclear Overhauser effects to be measured on the resonances of nearby protons. The assignments of resonances reported previously have been examined, and most have been confirmed. In conjunction with spin-decoupling methods, new assignments could be made so that assignments for some 70 resonances of 25 residues in lysozyme are now known. A high correlation was observed between the observed nuclear Overhauser effects and interproton distances calculated from cyrystallographic data. This indicates that the average structure of this region of lysozyme in the crystalline state is maintained in solution, that substantial populations of structures very different from this do not exist, and that the nuclear Overhauser technique can be applied in a straightforward manner to obtain structural data in solution at the 1-A level.
溶菌酶（EC 3.2.1.17）疏水盒区域残基的特定质子核磁共振（NMR）信号饱和，使得能够测量附近质子共振上的负核Overhauser效应。先前报道的共振归属已得到检验，大部分已得到确认。结合自旋去耦方法，可以进行新的归属，因此现在已知溶菌酶中25个残基的约70个共振的归属。观察到的核Overhauser效应与根据晶体学数据计算的质子间距离之间存在高度相关性。这表明溶菌酶该区域在晶体状态下的平均结构在溶液中得以保持，不存在与该结构非常不同的大量结构群体，并且核Overhauser技术可以直接应用于在埃级水平获得溶液中的结构数据。
