Regulation of Channel Function Due to Coupling with a Lipid Bilayer
Regulation of membrane protein functions due to hydrophobic coupling with a lipid bilayer is investigated. An energy formula based on the screened Coulomb interaction approximation has been developed between lipid bilayer and integral ion channels with different structures. We find
that the hydrophobic bilayer thickness channel length mismatch induces channel destabilization exponentially while negative lipid curvature linearly. Experimental parameters related to channel dynamics are consistent with theoretical predictions. This study provides a new insight that provides
better understanding of the underlying mechanisms of membrane protein functions in biological systems.
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Keywords: ION CHANNEL; LIPID BILAYER; MEMBRANE PROTEIN; SCREENED COULOMB INTERACTION
Document Type: Research Article
Publication date: April 1, 2012
- Journal of Computational and Theoretical Nanoscience is an international peer-reviewed journal with a wide-ranging coverage, consolidates research activities in all aspects of computational and theoretical nanoscience into a single reference source. This journal offers scientists and engineers peer-reviewed research papers in all aspects of computational and theoretical nanoscience and nanotechnology in chemistry, physics, materials science, engineering and biology to publish original full papers and timely state-of-the-art reviews and short communications encompassing the fundamental and applied research.
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