CEN Webinars: Stronger Bonds

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


Stu Borman
Senior Correspondent


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

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Register FREE at http://tinyurl.com/cm2jp7g