¹⁵N detection harnesses the slow relaxation property of nitrogen: Delivering enhanced resolution for intrinsically disordered proteins.

ABSTRACT: Studies over the past decade have highlighted the functional significance of intrinsically disordered proteins (IDPs). Due to conformational heterogeneity and inherent dynamics, structural studies of IDPs have relied mostly on NMR spectroscopy, despite IDPs having characteristics that make them challenging to study using traditional ¹H-detected biomolecular NMR techniques. Here, we develop a suite of 3D ¹⁵N-detected experiments that take advantage of the slower transverse relaxation property of ¹⁵N nuclei, the associated narrower linewidth, and the greater chemical shift dispersion compared with those of ¹H and ¹³C resonances. The six 3D experiments described here start with aliphatic ¹H magnetization to take advantage of it

SUBMITTER: Chhabra S 

PROVIDER: S-EPMC5828609 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature