Integrating ¹⁹F Distance Restraints for Accurate Protein Structure Determination by Magic Angle Spinning NMR Spectroscopy.

ABSTRACT: Traditional protein structure determination by magic angle spinning (MAS) solid-state NMR spectroscopy primarily relies on interatomic distances up to 8 Å, extracted from ¹³C-, ¹⁵N-, and ¹H-based dipolar-based correlation experiments. Here, we show that ¹⁹F fast (60 kHz) MAS NMR spectroscopy can supply additional, longer distances. Using 4F-Trp,U-¹³C,¹⁵N crystalline Oscillatoria agardhii agglutinin (OAA), we demonstrate that judiciously designed 2D and 3D ¹⁹F-based dipolar correlation experiments such as (H)CF, (H)CHF, and FF can yield interatomic distances in the 8-16 Å range. Incorporation of fluorine-based restraints into structure calculation improved the precision of Trp side chain conformations as wel

SUBMITTER: Runge BR 

PROVIDER: S-EPMC11674370 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature