Rapid folding of calcium-free subtilisin by a stabilized pro-domain mutant.

@article{Ruan1999RapidFO,
  title={Rapid folding of calcium-free subtilisin by a stabilized pro-domain mutant.},
  author={Biao Ruan and Jemima Hoskins and Philip N. Bryan},
  journal={Biochemistry},
  year={1999},
  volume={38 26},
  pages={
          8562-71
        }
}
In vitro folding of mature subtilisin is extremely slow. The isolated pro-domain greatly accelerates in vitro folding of subtilisin in a bimolecular reaction whose product is a tight complex between folded subtilisin and folded pro-domain. In our studies of subtilisin, we are trying to answer two basic questions: why does subtilisin fold slowly without the pro-domain and what does the pro-domain do to accelerate the folding rate? To address these general questions, we are trying to characterize… CONTINUE READING
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