Characterizing Protein-Nucleic Acid Interactions by Light Scattering
Presented Live: August 21, 2018
Harnessing the interactions between DNA, RNA, and proteins holds much promise for detecting biomarkers, diagnosing disease, and improving cancer-targeting therapeutics. Quantifying these interactions is essential for understanding and controlling their biomolecular mechanisms. Multi-angle light scattering (MALS) is a powerful tool for directly measuring molar masses of proteins, nucleic acids, and complexes in solution without fluorescent or radio labeling.
In this webcast, an expert will present two complementary light-scattering techniques for determining the stoichiometry and affinity of interactions between proteins and nucleic acids:
- Size-exclusion chromatography coupled with MALS, ultraviolet, and differential refractive index detection (SEC–MALS) analyzes each of the species present in a solution of macromolecules
- Composition-gradient MALS (CG–MALS) quantifies the binding affinity and stoichiometry of biomolecular complexes, including multi-step reactions, label-free, and immobilization-free
Application examples will focus on protein-DNA and protein-RNA complexes.