Fig. 1
From: Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway
Schematics of the NMR-detected H/D exchange experiment. The sample is incubated at elevated temperatures, resulting in a gradual temperature-dependent increase of the solvent-accessible surface with amide protons at exposed sites exchanging for deuterons, and subsequently cooled down for SSNMR detection. This cycle is repeated for each elevated temperature point to form a series of NMR spectroscopic snapshots which follow the unfolding pathway. Blue color represents exchanged parts of the protein
