Line Narrowing in Methyl-TROSY Using Zero-Quantum 1H-13C NMR Spectroscopy

Abstract
An enhanced sensitivity zero-quantum correlation experiment is proposed for recording 1H-13C correlations of methyl groups in highly deuterated, methyl protonated large proteins. The zero-quantum spectra benefit from TROSY-effects in which both intra- and inter-methyl dipolar relaxation interactions are minimized. Applications to malate synthase G at 5 °C (81 kDa single polypeptide chain enzyme, correlation time of 118 ns) and lysine decarboxylase at 45 °C (810 kDa decameric enzyme) are presented showing significant improvements in resolution relative to corresponding HMQC data sets, with only slight decreases (∼10%) in sensitivity.

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