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A very thermostable variant of the thermolysin-like protease from Bacillus stearothermophilus (G8C/N60C) was previously created by introduction of a disulfide bond into the cysteine-free pseudo-wild type variant (pWT) and thus fixing the unfolding region 56–69. In the present paper, we show that G8C/N60C and pWT can be reactivated from the completely unfolded states, accessible at ≥7.5M guanidine...
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