Interactions between proteins and nucleic acids often result in binding stoichiometries greater than 1:1 and may exhibit cooperativity, allosteric hindrance, or other complex phenomena. Quantifying the affinity and stoichiometry of these biomolecular assemblies is key to understanding the mechanism of interaction and to developing therapeutics that target and modulate them.
This white paper presents the characterization of protein-DNA complexes using two complementary multi-angle light scattering (MALS) techniques: 1) in combination with size exclusion chromatography
(SEC-MALS) and protein conjugate analysis to measure the overall complex molar mass and fraction of DNA and 2) composition-gradient MALS (CG-MALS) to quantify the stoichiometry and affinity at each binding site in the complex formation.
To download your copy of this application note complete the form opposite.
Registrants for this application note are covered by the Eclipse Business Media Privacy Policy.
Eclipse Business Media Ltd, Regd in England, No. 06513189, Woodview, Bull Lane Industrial Estate, Sudbury, CO10 0FD, United Kingdom, T +44 (0)161 818 7434, info@sepscience.com
Eclipse Business Media Ltd needs the contact information you provide to us to contact you about our products and services. You may unsubscribe from these communications at any time. For information on how to unsubscribe, as well as our privacy practices and commitment to protecting your privacy, check out our Privacy Policy or contact privacy@labxmediagroup.com
Copyright © 2023. All rights reserved