Many proteins rely on oligomerization — the assembly of multiple protein subunits into larger functional complexes — to regulate biological activity, facilitate molecular interactions, and carry out essential cellular processes. Because shifts in oligomeric state can influence both normal physiology and disease development, understanding how and why proteins assemble has become an important focus of modern biological research.
This application note explores how automated mass photometry enables researchers to characterize protein oligomerization under native conditions, quantify changes in assembly states, and investigate how environmental factors and molecular effectors influence protein behavior.
Download this application note to learn:
- How mass photometry helps identify monomeric, dimeric, and higher-order oligomeric protein species
- How to assess the effects of protein concentration, small-molecule inhibitors, and calcium on oligomerization dynamics
- How automation can improve reproducibility and accelerate screening of multiple experimental conditions
