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- W2031278106 abstract "For a complete understanding of biomolecular functions, electrostatic interactions have to be characterized. These interactions are highly dependent on the relative permittivity of the surrounding medium, including the interior of proteins and binding site regions. However, determination of the relative permittivity is not trivial. Here, we present an experimental method for measuring such physical properties by determining the microenvironmental dielectric constants of the protein acetylcholinesterase, which are 5.79 ± 0.10 for the whole protein interior and 3.72 ± 0.33 for the active site/gorge region. Exact experimental dielectric constant values can improve predictions from molecular dynamics and ligand electrostatic steering simulations and consequently contribute to a better understanding of the fast hydrolysis of acetylcholinesterase." @default.
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- W2031278106 date "2009-12-15" @default.
- W2031278106 modified "2023-10-16" @default.
- W2031278106 title "Determination of the Relative Permittivity of Acetylcholinesterase" @default.
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- W2031278106 doi "https://doi.org/10.1021/jz900261z" @default.
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