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

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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.