Referenced in: none

Automatically associated channels: Kv1.3

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

Authors: Christian Ader, Robert Schneider, Karsten Seidel, Manuel Etzkorn, Stefan Becker, Marc Baldus

Journal, date & volume: J. Am. Chem. Soc., 2009 Jan 14 , 131, 170-6

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/19063626

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.