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Inside Cover: Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion (Angew. Chem. Int. Ed. 46/2011)

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Abstract

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Molecular dynamics are generally anisotropic in nature. For the case of a three-site jump motion of a protein side chain (shown for valine), the apparent dipolar coupling tensor (turquoise/red lobes) therefore becomes asymmetric. In their Communication on page 11 005 ff., B. H. Meier, M. Ernst et al. report the first direct measurement of such asymmetric dipolar coupling tensors using isotopic labeling and REDOR solid-state NMR spectroscopy (REDOR data shown in the center).

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