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  Multiple binding sites for fatty acids on the potassium channel KcsA.

Bolivar, J. H., Smithers, N., East, J. M., Marsh, D., & Lee, A. G. (2012). Multiple binding sites for fatty acids on the potassium channel KcsA. Biochemistry, 51(13), 2889-2898. doi:10.1021/bi300153v.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-A044-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C774-C
Genre: Journal Article

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Bolivar, J. H., Author
Smithers, N., Author
East, J. M., Author
Marsh, D.1, Author              
Lee, A. G., Author
Affiliations:
1Emeritus Group of Spectroscopy and Photochemical Kinetics, MPI for Biophysical Chemistry, Max Planck Society, ou_578625              

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 Abstract: Interactions of fatty acids with the potassium channel KcsA were studied using Trp fluorescence quenching and electron paramagnetic resonance (EPR) techniques. The brominated analogue of oleic acid was shown to bind to annular sites on KcsA and to the nonannular sites at each protein − protein interface in the homotetrameric structure with binding constants relative to dioleoylphosphatidylcholine of 0.67 ± 0.04 and 0.87 ± 0.08, respectively. Mutation of the two Arg residues close to the nonannular binding sites had no effect on fatty acid binding. EPR studies with a spin-labeled analogue of stearic acid detected a high-affinity binding site for the fatty acid with strong immobilization. Fluorescence quenching studies with the spin-labeled analogue showed that the binding site detected in the EPR experiments could not be one of the annular or nonannular binding sites. Instead, it is proposed that the EPR studies detect binding to the central hydrophobic cavity of the channel, with a binding constant in the range of ∼ 0.1 − 1 μ M

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Language(s): eng - English
 Dates: 2012-03-122012-04-03
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/bi300153v
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Title: Biochemistry
Source Genre: Journal
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Pages: - Volume / Issue: 51 (13) Sequence Number: - Start / End Page: 2889 - 2898 Identifier: -