# Behe Meets the Peaceful Science Forum

**URL:** <https://discourse.peacefulscience.org/t/behe-meets-the-peaceful-science-forum/13294>\
**Category:** Public Square\
**Tags:** Science, Design, Society\
**Created:** [March 2, 2021, 11:03pm UTC](https://discourse.peacefulscience.org/t/behe-meets-the-peaceful-science-forum/13294 "2021-03-02T23:03:44Z")\
**Posts on this page:** 1\
**Showing post:** 44

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**Author:** ![Rumraket](https://sea2.discourse-cdn.com/flex016/user_avatar/discourse.peacefulscience.org/rumraket/32/9328_2.png) [@Rumraket](https://discourse.peacefulscience.org/u/Rumraket)\
**Post date:** [March 6, 2021, 8:46pm UTC](https://discourse.peacefulscience.org/t/behe-meets-the-peaceful-science-forum/13294/44 "2021-03-06T20:46:18Z")

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> [@swamidass](#):
>
> If I’m wrong here, I still don’t think that increasing protein stability would be a vanishingly unlikely event.

We had [a thread about this](https://discourse.peacefulscience.org/t/detwiler-questions-behe-polyphen-and-ratchets/5088/67) back shortly after I had first joined this forum. Roughly 15 to 30% of random mutations in proteins are stability increasing, with the remaining 70-85% being destabilizing. See:

> **[Universal distribution of mutational effects on protein stability, uncoupling...](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4770899/)**
>
> Robustness to destabilizing effects of mutations is thought of as a key factor of protein evolution. The connections between two measures of robustness, the relative core size and the computationally estimated effect of mutations on protein stability...

 ![Image1](https://us1.discourse-cdn.com/flex016/uploads/peacefulscience/original/2X/a/afb1ad18737baa9ee736950950b413538392ed58.jpeg)

Needless to say, **one in seven to one in three** aren’t bad odds at all. For hyperthermophile organisms, the percentage of mutations that are stabilizing on protein structure is on the lower end (~10%), as you would expect since they have already evolved for a long time under selection for high thermostability.

Now it has to be said, and this is extremely important to understand, that protein stability is not directly proportional to protein function. A protein can become both too stable and too unstable to function properly. A degradation/reduction in protein stability thus cannot automatically be said to constitute a degradation in protein functional capacity. So even if polar bear APOB mutations can be identified which is predicted by some algorithm to result in a reduction in protein stability, that does not imply the protein is suffering a degradation in it’s functional capacity.

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