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Mapping Protein Binding Affinities with Mass Photometry 

Learn how to apply mass photometry to calculate KD values for complex protein solutions using label-free bioanalytics 

Protein interactions serve as the cornerstone of functionality, yet their complexity often defies easy characterization. Mass photometry is a tool that can shed light on these intricate dynamics. By directly measuring the molecular mass of individual biomolecules in solution, mass photometry accurately identifies binding partners, complexes formed, and the strength of their affinities. 

Mapping Protein Binding Affinities with Mass Photometry

In this white paper, explore a recent study that uses mass photometry to shed light on how human and bovine Immunoglobulin G (IgG) antibodies interact with protein A. By revealing distinct variations in complex formation and binding strengths, this label-free technique offers a deeper understanding of critical biological mechanisms. 

Discover more about how mass photometry resolves complex equilibria, ensuring accurate quantification and assessment of protein-protein interactions. From unraveling intricate binding affinities to assessing sample homogeneity and purity, this technology is pivotal to understanding how proteins function together, and are affected by different conditions. 

Download this whitepaper to learn:

  • The intricacies of protein-protein interactions and how these can be quantified using mass photometry
  • How mass photometry resolves complex equilibria, aiding in precise quantification
  • Practice applications and implications of protein binding affinity quantifications in research and biotechnology

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