Structural analysis of the transient state of an enzyme active site using NMR relaxation dispersion

利用pf1噬菌体或丙烯酰胺凝胶作为对准介质，沿静磁场对几丁质酶进行对准。在此状态下观察到残余偶极耦合，证实了该系统对分析是有效的。为了进一步将弛豫色散方法应用于对准系统，我们使用了一个众所周知处于构象交换中的复杂系统。在改变配合物的化学计量量后，观察到残余偶极耦合也随之改变。

An enzyme chitinase was aligned along the static magnetic field using Pf1-phage or acrylamide gel as an alignment medium. In this state residual dipolar coupling was observed, confirming that the system was effective for the analysis. To further apply the relaxation dispersion method to the alignment system, a complex system which was well known to be in a conformational exchange was used. Upon changing the stoichiometry in the complex, it was observed that the residual dipolar coupling also changed accordingly.