Abstract
A combination of gradient-purged isotope-filtered NMR experiments is presented, which allows for the detection of long-lived bound water molecules in proteins. The discrimination of direct water–protein exchange from NOE effects between bound water and protein protons is achieved by NOE/ROE cancellation during the mixing time in one of the otherwise identical experiments. The method was applied successfully to 13 C/ 15 N -labelled serine protease PB92, and allowed for the identification of 22 protein–water NOEs in this 269-residue enzyme.
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