Nuclear magnetic resonance (NMR) has a long history of addressing mechanistic questions in membrane biology. Its unique capabilities include the non-perturbing nature of isotope labels, the ability of NMR signals to provide atomic-level structural and dynamic information in complex samples, including living systems, and the ability to detect very weak binding through chemical shift changes. Solution and solid-state NMR methods are highly complementary and enable a wide range of biomolecular complexity and dynamic timescales to be analyzed. Here we describe recent advances that push the envelope of current technology and offer new opportunities for targeting membrane protein assemblies to gain fundamental human health insights.
Shin et al. (Thu,) studied this question.