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Direct Detection of 3hJNC′ Hydrogen-Bond Scalar Couplings in Proteins by Solid-State NMR Spectroscopy

Authors


  • This work was financially supported by the Swiss National Science Foundation and the ETH Zürich. P.S. acknowledges an ETH fellowship.

Abstract

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Hydrogen bonds are ubiquitous interactions in proteins, and are important for their folding and functionality. Scalar coupling constants across hydrogen bonds in the protein backbone, some as small as 0.5 Hz, can be directly measured in the solid state by NMR spectroscopy (see figure). The nuclei on both sides of the hydrogen bond can be identified and the size of the coupling constant can be measured accurately.

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