Two-dimensional ¹⁹F-¹³C correlation NMR for ¹⁹F resonance assignment of fluorinated proteins.

ABSTRACT: ¹⁹F solid-state NMR is an excellent approach for measuring long-range distances for structure determination and for studying molecular motion. For multi-fluorinated proteins, assignment of ¹⁹F chemical shifts has been traditionally carried out using mutagenesis. Here we show 2D ¹⁹F-¹³C correlation experiments that allow efficient assignment of the ¹⁹F chemical shifts. We have compared several rotational-echo double-resonance-based pulse sequences and ¹⁹F-¹³C cross polarization (CP) for 2D ¹⁹F-¹³C correlation. We found that direct transferred-echo double-resonance (TEDOR) transfer from ¹⁹F to ¹³C and vice versa outperforms out-and-back coherence transfer schemes. ^19<

SUBMITTER: Shcherbakov AA 

PROVIDER: S-EPMC7445029 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature