Abstract
A simple approach for detecting internal water molecules in proteins in solution is described. This approach combines 19F-detected heteronuclear Overhauser and exchange spectroscopy (HOESY) with site-specific 19F substitution. The model system employed was intestinal fatty acid-binding protein complexed with [2-mono-19F]-palmitate. An intense cross peak was observed between the fluorine and a buried water molecule, as defined in the 1.98 Å crystal structure of the complex. From HOESY spectra, the fluorine-water distance was estimated to be 2.1 Å, in agreement with the crystal structure. This approach may be applicable to macromolecules that are too large for 1H-detected NMR methods.
Original language | English |
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Pages (from-to) | 415-419 |
Number of pages | 5 |
Journal | Journal of Biomolecular NMR |
Volume | 5 |
Issue number | 4 |
DOIs | |
State | Published - Jun 1995 |
Keywords
- Bound water
- Fatty acid-binding protein
- HOESY NMR
- Proteins