Abstract
YbeA is a hypothetic methyltransferases (MTases) enzyme. X‐ray crystallography study indicated that the backbone of this protein form a deep trefoil knot. It is interesting to reveal the mechanism of knot transition during its folding process. In this study we have cloned, expressed and folded this protein from inclusion body of E. coli. The conformational analysis of its unfolded, folding intermediates and native form, by spectrophotometers, and dynamic light scattering indicated that YbeA is a native knot protein. There is no knot transition during the folding process. Meanwhile, this deep knot protein makes itself thermal stable in high temperature environment (above 125 °C) which was analyzed by differential scanning calorimeter. Therefore, this knot structure may be used in thermal stable enzyme engineering.
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