Structural rearrangements of membrane proteins probed by water-edited solid-state NMR spectroscopy.
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.
Ader
Christian
C
Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Schneider
Robert
R
Seidel
Karsten
K
Etzkorn
Manuel
M
Becker
Stefan
S
Baldus
Marc
M
D001426:Bacterial Proteins / Q000737:chemistry*; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D025602:Halorhodopsins / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D015221:Potassium Channels / Q000737:chemistry*; D025603:Sensory Rhodopsins / Q000737:chemistry*; D014867:Water / Q000737:chemistry; D000099211:Phospholamban
D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; D025602:Halorhodopsins; D008051:Lipid Bilayers; D015221:Potassium Channels; D025603:Sensory Rhodopsins; D014867:Water; D000099211:Phospholamban; C107790:prokaryotic potassium channel; C061508:sensory rhodopsin II protein, archaeal