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Application note: Mass photometry in denaturing conditions
Learn how mass photometry can monitor protein stability. Discover how it can provide valuable insights into protein unfolding and refolding processes, even when traditional bulk methods fall short. Explore a case study involving the reversible unfolding of enolase, to understand how mass photometry excels in monitoring the denaturation and renaturation of proteins within multimeric complexes. Learn also what is the impact of denaturant concentrations on optical measurements and the strategies to overcome challenges.
Additional resources
APPLICATION NOTE: Quantifying protein binding affinities using mass photometry
Read this application note to learn how you can use the TwoMP mass photometer to characterize protein-protein interactions, quickly and easily. Discover how you can determine the relative abundance of each protein and the complexes they form in solution, using this label-free bioanalytical tool. Learn also how you can use the mass photometry measurements to calculate the equilibrium dissociation constant (KD) for each interaction.
APPLICATION NOTE: Characterization of protein interaction equilibria
Learn how mass photometry can be applied to the study of complex equilibrium formation reactions and assess how changes in the chemical environment or protein concentration affect equilibria. More specifically, discover how mass photometry can be used to study the oligomerization process of a recombinant protein that forms tetramers. Using this multimeric protein as an example, learn how to measure the relative abundances of each oligomeric species across a range of physiologically relevant protein concentrations and assess the effect of environmental factors (such as temperature) on reaction equilibria.
