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Many researchers, even academic scientists, don't characterize protein stability at all in their laboratories. Too o en,
researchers will assume the protein's molecular weight provides the information they need, unaware that stability
can lead to unreliable or irreproducible data. For antibody development, an important branch of protein-based
drug discovery, researchers must remain aware of their protein's stability from the beginning of development, as it
constitutes the second most critical criterion for drug selection behind its binding properties. [Read our ebook on
measuring binding affinity]
Characterizing protein stability is not only important for drug discovery, but also for quality control for drug production.
Protein stability measurements are an important part of the process of producing and testing the candidate and
eventually the final product. A destabilized protein may denature before it it reaches the patient, wherein it can be
ineffective, or even cause harm.
To measure a protein's stability, you need to look at how the protein unfolds. There are basically two methods
commonly used to cause protein unfolding––thermal and chemical treatments. Thermal unfolding involves exposing a
target molecule to a defined temperature gradient, which causes the molecule to denature. The temperature at which
the protein unfolds is an index of the protein's stability: The higher the unfolding temperature, the more stable it is.
Exposing a protein to a thermal gradient can also cause it to aggregate. This occurrence might indicate that the change
in temperature caused the protein to unfold or misfold and this can also serve as a way to characterize the stability of a
protein.
When do I characterize
protein stability?
How do I characterize
protein stability?
