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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Calcium-Binding Proteins / chemistry*
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Halorhodopsins / chemistry*
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Lipid Bilayers / chemistry*
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Models, Chemical
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Models, Molecular
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Nuclear Magnetic Resonance, Biomolecular / methods*
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Potassium Channels / chemistry*
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Sensory Rhodopsins / chemistry*
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Water / chemistry
Substances
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Bacterial Proteins
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Calcium-Binding Proteins
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Halorhodopsins
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Lipid Bilayers
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Potassium Channels
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Sensory Rhodopsins
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phospholamban
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prokaryotic potassium channel
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sensory rhodopsin II protein, archaeal
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Water