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Electric migration of α‐hemolysin in supported n ‐bilayers: A model for transmembrane protein microelectrophoresis
Author(s) -
Harb Frédéric,
Tinland Bernard
Publication year - 2013
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201300202
Subject(s) - electrophoresis , microelectrophoresis , electric field , transmembrane protein , chemistry , bilayer , lipid bilayer , biophysics , chemical physics , radius , isoelectric point , membrane protein , membrane , analytical chemistry (journal) , crystallography , materials science , chromatography , biochemistry , physics , biology , computer science , receptor , quantum mechanics , enzyme , computer security
Proteome analysis involves separating proteins as a preliminary step toward their characterization. This paper reports on the translational migration of a model transmembrane protein (α‐hemolysin) in supported n ‐bilayers ( n , the number of bilayers, varies from 1 to around 500 bilayers) when an electric field parallel to the membrane plane is applied. The migration changes in direction as the charge on the protein changes its sign. Its electrophoretic mobility is shown to depend on size and charge. The electrophoretic mobility varies as 1/ R 2 , with R the equivalent geometric radius of the embedded part of the protein. Measuring mobilities at differing pH in our system enables us to determine the p I and the charge of the protein. Establishing all these variations points to the feasibility of electrophoretic transport of a charged object in this medium and is a first step toward electrophoretic separation of membrane proteins in n ‐bilayer systems.