9.2 years ago by
Maastricht, The Netherlands
As far as I know, no, not really.
Activity measurements are indeed influenced by temperature, and different from direct chemical activities which show an ongoing and exponential increase in speed at increasing temperatures enzyme reactions have a temperature optimum. That is indeed largely caused by loss of conformation at higher temperatures, but that is not the same as thermostability. Normally you don't measure conformation changes or folding, although you can traditionally for instance through measurement of changes in optical rotation. What you do measure is product formation of substrate consumption, sometimes indirectly. Conformation loss is often reversible. You can off course access that by first increasing the temperature and then decreasing it again. Which is indeed a classical biochemical approach. But you need that type of data to estimate stability from activity. Oftentimes irreversible conformation loss also leads simply to precipitation (although not in the presence of high urea concentrations).
A bioinformatics approach to estimate one from the other is thus not very useful. It would be interesting to know in how far direct estimations of stability can be made from the protein structure. If the latter question is what you really wanted to ask the question does indeed have a bioinformatics aspect (I could imagine people doubt that and see it as a pure wetlab question), but I don't know the answer to that part.