Hello! These days, I'm working on enzyme modification to enhance the stability of proteins. I've encountered a question when using mutation prediction programs like Dynamut and Cupsat. Despite having a negative DDG value, it is labeled as "destabilizing." According to my understanding, a negative DDG value indicates improved stability. Could you clarify the precise meaning of these values? Does a negative DDG value mean that introducing the mutation results in increased stability, or does it mean the opposite, indicating destabilization?
Dear Tae-Hun Kim Not sure how you concluded that a negative value is stabilizing but the paper describing Dynamut clearly state: “Since this definition can vary across the methods and for comparison purposes we defined (delta delta)G ≥ 0 as stabilizing and (delta delta)G < 0 as destabilizing”Article DynaMut: Predicting the impact of mutations on protein confo...
Best regards.
It depends on whether you consider deltaG of folding or unfolding for quantifying protein stability
Also, mutations are expensive. Consider glycosylation or phorphorylations that are easier and cheaper. They can increase stability in hydrophilic media. If you want the enzyme to be immobilized at a later stage, covalent modification is a serious candidate for consideration. Important to remember that destabilization is also environment dependent.
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