Direct detection of carbon and nitrogen nuclei for high-resolution analysis of intrinsically disordered proteins using NMR spectroscopy.

ABSTRACT: Nuclear magnetic resonance spectroscopy (NMR) is a powerful technique for characterizing the structural and dynamic properties of intrinsically disordered proteins and protein regions (IDPs & IDRs). However, the application of NMR to IDPs has been limited by poor chemical shift dispersion in two-dimensional (2D) ¹H-¹⁵N heteronuclear correlation spectra. Among the various detection schemes available for heteronuclear correlation spectroscopy, ¹³C direct-detection has become a mainstay for investigations of IDPs owing to the favorable chemical shift dispersion in 2D ¹³C'-¹⁵N correlation spectra. Recent advances in cryoprobe technology have enhanced the sensitivity for direct detection of both ¹³C and ¹⁵N resonances

SUBMITTER: Gibbs EB 

PROVIDER: S-EPMC5984115 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature