Synthetic nanodiscs mimic native membranes, stabilizing receptors that would otherwise unravel during purification. Yet scaling up introduces an operational frustration: the protective polymer matrix hides the underlying protein structures, allowing standard purification profiles to appear uniform even when a fraction contains intact complexes, vacant discs, and fragments.
This application note demonstrates how single-molecule mass tracking quantifies the exact ratio of target-loaded complexes to empty discs. By measuring the light scattering of individual particles rather than bulk ensemble averages, the data equips researchers to identify the highest-purity fraction before committing a sample to grid preparation.
Download the application note to
- See how measuring in native copolymers eliminates the background noise of detergent micelles
- Review side-by-side data showing how identical light scattering traces conceal different structural distributions
- Examine the protocol for determining intact complex mass and antibody binding stoichiometry in under a minute
