Paramagnetic NMR to study iron sulfur proteins: ¹³C detected experiments illuminate the vicinity of the metal center.

ABSTRACT: The robustness of NMR coherence transfer in proximity of a paramagnetic center depends on the relaxation properties of the nuclei involved. In the case of Iron-Sulfur Proteins, different pulse schemes or different parameter sets often provide complementary results. Tailored versions of HCACO and CACO experiments significantly increase the number of observed C^α/C' connectivities in highly paramagnetic systems, by recovering many resonances that were lost due to paramagnetic relaxation. Optimized ¹³C direct detected experiments can significantly extend the available assignments, improving the overall knowledge of these systems. The different relaxation properties of C^α and C' nuclei are exploited in CACO vs COCA experiments and the complementarity of the two

SUBMITTER: Querci L 

PROVIDER: S-EPMC10687126 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature