⁷⁷Se-¹³C based dipolar correlation experiments to map selenium sites in microcrystalline proteins.

ABSTRACT: Sulfur-containing sites in proteins are of great importance for both protein structure and function, including enzymatic catalysis, signaling pathways, and recognition of ligands and protein partners. Selenium-77 is an NMR active spin-1/2 nucleus that shares many physiochemical properties with sulfur and can be readily introduced into proteins at sulfur sites without significant perturbations to the protein structure. The sulfur-containing amino acid methionine is commonly found at protein-protein or protein-ligand binding sites. Its selenium-containing counterpart, selenomethionine, has a broad chemical shift dispersion useful for NMR-based studies of complex systems. Methods such as (¹H)-⁷⁷Se-¹³C double cross polarization or {⁷⁷Se}-¹³

SUBMITTER: Quinn CM 

PROVIDER: S-EPMC9195563 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature