The potentialities of a 2D proton-detected heteronuclear exchange experiment to assign the nitrogen and amide proton resonances in a uniformly 15 N-enriched macromolecule involved in a complex, starting from the free form assignments, are demonstrated on a protein-DNA complex. This 2D experiment is
Editing of Chemical Exchange-Relayed NOEs in NMR Experiments for the Observation of Protein–Water Interactions
✍ Scribed by Giuseppe Melacini; Robert Kaptein; Rolf Boelens
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 72 KB
- Volume
- 136
- Category
- Article
- ISSN
- 1090-7807
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✦ Synopsis
An experimental approach for the editing of exchange-relayed NOEs in water-selective NOE experiments is presented. The proposed pulse sequence is based on the application during the NOE mixing time of continuous wave irradiation, which saturates resonances of relaying labile protons in slow chemical exchange with water. The technique can efficiently reduce the contributions of exchange-relayed NOE peaks that often crowd the water-selective NOE spectra and hide direct intermolecular NOEs between water and protein protons. The present approach opens new opportunities for the characterization of hydration by NMR, even in the proximity of polar labile groups.
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