For understanding of the function of domain, I removed small domain ( with 7 beta sheet) from my enzyme. my enzyme( cellulase) has two domain that the catalic domain is major domain.
I check thermostability of wild-type and truncated enzyme, my data showed thermostability increased. Why?
It is not unusual that protein domains get destabilized by other neighbouring domains. Remember nature made proteins to serve for certain function not to be most stable.
One example you can find in this paper: http://www.jbc.org/content/285/30/22831.long
There figure 3 shows that A3 is destabilized when in a construct with neighbouring domains. As soon as you isolate A3 it is more stable than in the complex.
Best regards.
Hello Alexander
thank you for answer
the molecular simulation showed that this domain has function in stability. but our result experimentally showed another thing.
it's interesting answer
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