the HUNK

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the HUNK

Make stability routine

The HUNK makes what wasn’t possible before — routine measurement of protein stability in different formulations using chemical denaturation — totally doable. It’ll up your insight into protein stability and let you know not only if your protein will aggregate, but also the pathway it’ll take — something you can’t do with any other single tool. Get brochure.

ΔG quantify stability

ΔGtrend aggregation pathway & propensity

Kd small molecule affinity

HunK

 

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Automate everything

The HUNK completely automates the chemical denaturation and protein stability measurement process. Easy set up in application-specific trays is all it takes to get started. Once the HUNK gets going, it’ll crank out up to 96 ΔGs on 96 different conditions fully unattended. With those ΔGs in hand, you’ll know right away whether or not it’s worth spending your time on minimizing aggregation or optimizing solubility and viscosity.

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Get ΔG in an hour

The HUNK’s got a much cooler way to get ΔG values. It adds increasing concentrations of denaturant to proteins until they completely unfold to get their denaturation curves. The midpoint of the curve, the C1/2, is the concentration of denaturant needed to onehalf unfold the protein. The HUNK multiplies that C1/2 by the slope (m value) of the curve at the C1/2 to get the ΔG for each of your proteins — and does it in about an hour.

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Fix aggregation

With one HUNK experiment, you’ll know if and how your protein could aggregate. Follow ΔG over increasing protein concentrations, and get the ΔGtrend. When ΔGtrend goes up, you might want to check out a native state aggregation fix. When ΔGtrend goes down, you’ve got denatured state aggregation to deal with. A flat ΔGtrend means you’re good to go. In one day, the HUNK gives you more info than ever before about your protein’s aggregation pathway.

aggregation

Learn more

The HUNK lets you identify the most stable formulations and proteins. Take a deeper dive into the HUNK’s published articles and background references on chemical denaturation and protein stability.

App Notes

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