Membrane proteins are traditionally solubilised and stabilised in solution by detergents.  Expedeon’s NVoy technology provides an alternative strategy, and has been demonstrated to maintain the solubility of a tagged membrane protein during buffer exchange into a detergent- and denaturant-free working buffer.  Far-UV circular dichroism analysis demonstrates that the membrane protein is both soluble and has retained structure during buffer exchange.

NV10 Maintains protein solubility Low wavelength penetration

Example 1: Far UV-CD spectrum of a tagged membrane protein demonstrating retained secondary structure.

Solubilising additives which suppress aggregation either distort the far-UV CD signal, by contributing a signal of their own, (L-arginine), or have poor UV transparency preventing accurate signal detection (NDSB).  A far-UV CD spectrum of lysozyme was collected, either in buffer alone, buffer with 0.8 x NV10, buffer containing 4 mM L-arginine or buffer containing 4 mM NDSB.
While the spectrum of lysozyme with NV10 is indistinguishable from that of lysozyme in buffer alone, the spectrum containing L-arginine has a distorted signal below 230 nm, while that containing NDSB cannot be collected below 215 nm.  In each of the latter cases the resulting spectra prevent secondary structure information from being collected.

With; NV10 - Spectrum is unaffected L-Arginine - Signal is distorted NDSB - Poor transparency