The use of 2D oriented membranes has been presented as a method for obtaining structural information from non-crystalline proteins in a biologically friendly environment. However, the functional properties of isolated membrane proteins cannot be probed using continuous lipid bilayers as several membrane proteins are reconstituted into the same lipid matrix. Nanodiscs are self-assembled nanostructures composed of a belt protein (MSP) and ~50 nm2 patch of lipid bilayer, in which single membrane proteins can be solubilised. We suggest that a 2D matrix of nanodiscs is a more appropriate choice of oriented membrane model.  Herein, we present how nanodiscs can be aligned in organized monolayers both at the solid-liquid and just below the air-water interface.  As a proof of concept neutron reflectivity and Quartz Crystal Micro-balance studies of the NADPH dependent conformational changes of cytochrome P450 reductase as a function of lipid bilayer charge and phase are presented.

Using nanodiscs as a plattform to study membrane protein function and structure on surfaces

243rd National Meeting (2012)

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