⁷⁷Se NMR Probes the Protein Environment of Selenomethionine.

ABSTRACT: Sulfur is critical for the correct structure and proper function of proteins. Yet, lacking a sensitive enough isotope, nuclear magnetic resonance (NMR) experiments are unable to deliver for sulfur in proteins the usual wealth of chemical, dynamic, and structural information. This limitation can be circumvented by substituting sulfur with selenium, which has similar physicochemical properties and minimal impact on protein structures but possesses an NMR compatible isotope (⁷⁷Se). Here we exploit the sensitivity of ⁷⁷Se NMR to the nucleus' chemical milieu and use selenomethionine as a probe for its proteinaceous environment. However, such selenium NMR spectra of proteins currently resist a reliable interpretation because systematic connections between variations of syst

SUBMITTER: Chen Q 

PROVIDER: S-EPMC8088340 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature