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Complementary Characteristics of Homologous p-octiphenyl β-Barrels with Ion Channel and Esterase Activity

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Published in Bioorganic & Medicinal Chemistry. 2003, vol. 11, no. 7, p. 1363-1369
Abstract We report that decreasing ß-sheet length in homologous multifunctional rigid-rod ß-barrels with internal histidines increases ion channel stability by three orders of magnitude, reduces binding activity by four orders of magnitude, and reduces esterase activity up to 22-times. These results are further used to evaluate methods employed to characterize suprastructure and activity of synthetic multifunctional pores formed by p-octiphenyl ß-barrels with emphasis on applicability of the Hille model to determine internal diameters and the Woodhull equation to locate internal active sites.
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SOM, Abhigyan, SAKAI, Naomi, MATILE, Stefan. Complementary Characteristics of Homologous p-octiphenyl β-Barrels with Ion Channel and Esterase Activity. In: Bioorganic & Medicinal Chemistry, 2003, vol. 11, n° 7, p. 1363-1369. https://archive-ouverte.unige.ch/unige:7014

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Deposited on : 2010-06-18

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