Structural Constraints from Proton-Mediated Rare-Spin Correlation Spectroscopy in Rotating Solids

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Abstract
A novel solid-state NMR concept is introduced that allows for the detection of through-space proton−proton contacts in high spectral resolution. The proposed method not only can be utilized to infer sequential assignments and backbone or side chain conformation in solid-phase polypeptides, but it also provides information about the three-dimensional arrangement of the molecule of interest. As a result, the molecular structure can be studied without additional restrictions regarding sample labeling or magic angle spinning rates.