Abstract
The lack of a membrane environment in membrane protein crystals is considered one of the major limiting factors to fully imply X-ray structural data to explain functional properties of ion channels [Gulbis, J.M. and Doyle, D. (2004) Curr. Opin. Struct. Biol. 14, 440-446]. Here, we provide infrared spectroscopic evidence that the structure and stability of the potassium channel KcsA and its chymotryptic derivative 1-125 KcsA reconstituted into native-like membranes differ from those exhibited by these proteins in detergent solution, the latter taken as an approximation of the mixed detergent-protein crystal conditions.
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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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Cell Membrane / chemistry*
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Cell Membrane / metabolism
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Detergents / chemistry
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Glucosides / chemistry
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Models, Molecular
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Potassium Channels / chemistry*
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Potassium Channels / genetics
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Potassium Channels / metabolism*
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Protein Structure, Quaternary*
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Spectroscopy, Fourier Transform Infrared
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Streptomyces lividans / chemistry*
Substances
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Bacterial Proteins
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Detergents
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Glucosides
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Peptide Fragments
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Potassium Channels
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Recombinant Proteins
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prokaryotic potassium channel
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dodecyl maltoside