J. Am. Chem. Soc., 2009, 131 (1), pp 170–176

Structural Rearrangements of Membrane Proteins Probed by Water-Edited Solid-State NMR Spectroscopy
Christian Ader, Robert Schneider, Karsten Seidel‡, Manuel Etzkorn, Stefan Becker‡ and Marc Baldus

Abstract

We show that water-edited solid-state NMR spectroscopy allows for probing global protein conformation and residue-specific solvent accessibility in a lipid bilayer environment. The transfer dynamics can be well described by a general time constant, irrespective of protein topology and lipid environment. This approach was used to follow structural changes in response to protein function in the chimeric potassium channel KcsA-Kv1.3. Data obtained as a function of pH link earlier biochemical data to changes in protein structure in a functional bilayer setting.