Native mass spectrometry transfers intact noncovalent assemblies from solution into the gas phase under gentle ionization and desolvation conditions, so stoichiometry and complex composition can be measured directly. In the analytical laboratory it complements denaturing mass spectrometry for questions about association state and ligand binding.

What native MS shows: Because complexes are preserved, researchers can observe oligomeric distributions, bound ligands or metals, and heterogeneity that denaturing workflows would erase. Reports should document source conditions, buffer composition and volatility, concentration, and calibration, because apparent stoichiometry depends on those experimental details.

Use in a QC workflow: Native MS is typically paired with HPLC purity testing, conventional high-resolution mass spectrometry, and size-based methods so identity, purity, and assembly findings are cross-checked by independent methods. Run reference standards and document sample preparation exactly.

Limitations: Native MS is a specialized technique sensitive to buffer and instrument tuning and does not replace quantitative purity or identity testing by HPLC and mass spectrometry; it supports those methods for questions they cannot answer alone.

Disclaimer: For laboratory research purposes only. Not for human consumption. The methods described are analytical laboratory techniques; no medical or therapeutic claim is made.

Citations: Standard native mass spectrometry methods literature for noncovalent biomolecular complexes.