Quantifying Affinity and Stoichiometry of Biomolecular Interactions
by Composition-Gradient Multi-Angle Light Scattering (CG-MALS)
Tuesday, April 23, 2013
USA 11:00 a.m. EDT / 10:00 a.m. CDT / 8:00 a.m. PDT / 16:00 BST
Who should attend?
• Protein chemists quantifying affinity and stoichiometry of protein-protein, protein-DNA, and other macromolecular interactions
• Scientists performing protein and peptide engineering, aptamer screening, and site-specific mutagenesis, and other directed evolution to engineer specific binding behavior
• Crystallography and NMR researchers identifying structure- function relationships, binding epitopes, and solution vs. crystal association states
• Laboratory Managers/Directors/Supervisors performing biophysical characterization
Sophia Kenrick, Ph.D.
Application Development Engineer
Wyatt Technology Corporation
Composition-gradient multi-angle static light scattering (CG-MALS) is a powerful, label-free technique for quantifying the affinity and stoichiometry of macromolecular interactions. CG-MALS measures interactions entirely in solution without tagging or immobilization, which can confound measurements by other techniques. In this webinar, we will demonstrate how CG-MALS has been successfully applied to the study of self- association, hetero-association with simple stoichiometry, and complex combinations of self- and hetero-association.
Key Learning Objectives:
• Brief review of static light scattering and how it can be applied to macromolecular interactions
• How Composition-Gradient Multi-Angle Light Scattering (CG-MALS) is a label free method that can be used to:
- Determine monomer molecular weight and self-association properties of macromolecules in solution
- Measure binding affinity and stoichiometry of protein-protein and protein- DNA interactions
- Quantify multivalent binding, cooperativity, and other complex interactions in solution