Duncan McGillivray
| Position |
Department / Business Unit |
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Department of Biophysics |
| Institution |
Disciplines |
| Johns Hopkins University |
Nanobiotechnology Physics |
| City |
State / Provence |
| Baltimore |
MD |
| Country |
Website |
| USA |
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| Fax |
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Solid-supported model membranes are particularly useful for studies of membrane proteins, as they open routes to investigations with surface-sensitive characterization techniques. We discuss a membrane system based upon a synthetic lipid that consists of alkyl tails attached through a glycerol to a thiolated polyethylene oxide spacer, which forms a mixed SAM with smaller “backfilling” mercaptoethanol molecules. Bilayer formation produces membranes which are electrochemically tight, particularly robust, and well suited to membrane protein incorporation because they allow the protein to occupy trans-membrane space. The system has been studied with a range of mutually supportive techniques, including electrochemical impedance spectroscopy (EIS), AFM, ellipsometry, and neutron reflectivity. Importantly we use the neutron reflectometry to show that the membrane also contains a sub-membrane solvent reservoir. The particular combination of electrochemical measurements and neutron reflection permits structural characterization of membrane proteins while simultaneously testing protein activity in this synthetic environment. Our results will focus on the membrane optimization, as well as results from early protein studies.
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