Leveraging relaxation-optimized ¹H-¹³C_F correlations in 4-¹⁹F-phenylalanine as atomic beacons for probing structure and dynamics of large proteins.

ABSTRACT: NMR spectroscopy of biomolecules provides atomic level information into their structure, dynamics and interactions with their binding partners. However, signal attenuation from line broadening caused by fast relaxation and signal overlap often limits the application of NMR to large macromolecular systems. Here we leverage the slow relaxation properties of ¹³C nuclei attached to ¹⁹F in aromatic ¹⁹F-¹³C spin pairs as well as the spin-spin coupling between the fluorinated ¹³C nucleus and the hydrogen atom at the meta-position to record two-dimensional ¹H-¹³C_F correlation spectra with transverse relaxation-optimized spectroscopy selection on ¹³C_F. To accomplish this, we synthesized [4-

SUBMITTER: Boeszoermenyi A 

PROVIDER: S-EPMC12805932 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature