When seeking to understand a protein construct or evaluate the performance of a formulation, the best candidates sometimes fail to distinguish themselves by thermal ramps, and common techniques can’t answer the critical question “what are my aggregates made of?” Quantifying a protein’s Gibbs free energy (ΔG) with Hunky gives you an orthogonal technique to gather real info on how rock-solid your protein is at ambient temperatures. And since ΔG is a measurement of protein equilibrium, the balance between folded and unfolded protein states is immediately known. Gathering ΔG data at 2 or more concentrations of a protein helps to decipher the most likely aggregation pathway – a bunch of native-state proteins, or a glob of unfolded ones.
In this webinar, Dr. Kevin Lance will walk through the advantages of using Hunky to measure ΔG as an orthogonal, room temperature, and quantitative technique to probe a protein’s stability. He will also explain the underlying concepts that let you see your protein’s aggregation pathway – without the need for lengthy experiments that can take weeks or months.
Key Learning Objectives
Understand how ΔG gives you insight into the equilibrium between folded and unfolded protein states
See how room temperature measurements of chemical stability can be an orthogonal asset to other protein stability metrics
Learn how testing ΔG at multiple concentrations gives you insight into protein aggregation behavior
Kevin Lance, PhD Product Manager Unchained Labs
Technology Networks Limited
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