Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway

Abstract

Studying the unfolding of membrane proteins in a native-like lipid environment is challenging. Here the authors describe a method combining hydrogen-deuterium exchange and solid-state NMR measurements that allows the characterization of unfolding events in lipid-embedded membrane proteins and use the photoreceptor Anabaena Sensory Rhodopsin as a test case.