Front Cover: Specific Signal Enhancement on an RNA‐Protein Interface by Dynamic Nuclear Polarization (Chem. Eur. J. 16/2023)

Abstract

Like bright stars in a dark sky, sparsely 13C-labeled methyl groups in the protein domain “illuminate” the binding pocket of a ribonucleoprotein (RNP) complex for specific solid-state NMR spectroscopy of the interaction surface by localized transfer of their hyperpolarization to 13C-labeled adenosines in the RNA domain. This is enabled by specific cross-relaxation enhancement by active motions under dynamic nuclear polarization (SCREAM-DNP) in combination with homonuclear dipolar recoupling. More information can be found in the Research Article by A. Marchanka, B. Corzilius and co-workers (DOI: 10.1002/chem.202203443).