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Structural rearrangements of membrane proteins probed by water-edited solid-state NMR spectroscopy

By C. Ader, R. Schneider, K. Seidel, M. Etzkorn, S. Becker and M. 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

Year: 2009
OAI identifier: oai:dspace.library.uu.nl:1874/43802
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