Probing internal water molecules in proteins using two-dimensional 19F-1H NMR

David P. Cistola, Kathleen B. Hall

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


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 languageEnglish
Pages (from-to)415-419
Number of pages5
JournalJournal of Biomolecular NMR
Issue number4
StatePublished - Jun 1995


  • Bound water
  • Fatty acid-binding protein
  • Proteins


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