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 13C/ 15N-labelled serine protease PB92, and allowed for the identification of 22 protein-water NOEs in this 269-residue enzyme.
Original languageEnglish
Pages (from-to)706-712
JournalChemical Physics Letters
Volume300
Issue number5
DOIs
Publication statusPublished - 1 Feb 1999

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