¹H-detected MAS solid-state NMR experiments enable the simultaneous mapping of rigid and dynamic domains of membrane proteins.

ABSTRACT: Magic angle spinning (MAS) solid-state NMR (ssNMR) spectroscopy is emerging as a unique method for the atomic resolution structure determination of native membrane proteins in lipid bilayers. Although ¹³C-detected ssNMR experiments continue to play a major role, recent technological developments have made it possible to carry out ¹H-detected experiments, boosting both sensitivity and resolution. Here, we describe a new set of ¹H-detected hybrid pulse sequences that combine through-bond and through-space correlation elements into single experiments, enabling the simultaneous detection of rigid and dynamic domains of membrane proteins. As proof-of-principle, we applied these new pulse sequences to the membrane protein phospholamban (PLN) reconstituted in lipi

SUBMITTER: Gopinath T 

PROVIDER: S-EPMC5764182 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature