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

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

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

J Biomol NMR. 1995 Jun;5(4):415-9

Authors: Cistola DP, Hall KB

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 A crystal structure of the complex. From HOESY spectra, the fluorine-water distance was estimated to be 2.1 A, in agreement with the crystal structure. This approach may be applicable to macromolecules that are too large for 1H-detected NMR methods.

PMID: 7647559 [PubMed - indexed for MEDLINE]



Source: PubMed