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Probing internal water molecules in proteins using two-dimensional19F-1H NMR

✍ Scribed by David P. Cistola; Kathleen B. Hall

Book ID: 104653704
Publisher: Springer Netherlands
Year: 1995
Tongue: English
Weight: 447 KB
Volume: 5
Category: Article
ISSN: 0925-2738
DOI: 10.1007/bf00182285

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✦ Synopsis

A simple approach for detecting internal water molecules in proteins in solution is described. This approach combines ~9F-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-~gF]-palmitate. An intense cross peak was observed between the fluorine and a buried water molecule, as defined in the 1.98 /k crystal structure of the complex. From HOESY spectra, the fluorine-water distance was estimated to be 2.1/k, in agreement with the crystal structure. This approach may be applicable to macromolecules that are too large for 1H-detected NMR methods.

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