Accurate characterization of proteins is fundamental to understanding their structure, function, and interactions. Yet protein samples rarely exist as uniform populations; instead, they often comprise dynamic mixtures of monomers, oligomers, and transient complexes. Common analytical techniques such as gel electrophoresis, size-exclusion chromatography, and dynamic light scattering rely on bulk measurements, which can mask this underlying heterogeneity and limit resolution.
This application note demonstrates how single-molecule mass photometry supports rapid, high-resolution characterization of protein samples by directly measuring molecular mass in solution, enabling detailed assessment of purity, heterogeneity, and oligomerization under native conditions.
Download this application note to learn:
- How single-molecule measurements reveal protein purity, oligomeric states, and sample heterogeneity with high resolution
- How buffer conditions, pH, and additives influence protein stability and complex formation
- How rapid, low-sample workflows can support more informed decisions before downstream structural and functional analyses
