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KMID : 0613819990090060733
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Journal of Life Science
1999 Volume.9 No. 6 p.733 ~ p.736
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Unfolding Property of Residue 24-Substituted Tryptophan Synthase α-Subunits
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Abstract
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The doubly altered mutant tryptophan synthase α-subunits, in which Thr 24 was replaced by Ser, Leu or Lys in addition to F139W substitution, were purified. Urea-induced unfolding equilibrium curves of these proteins, monitored by fluorescence intensity of tryptophan, show that the alterations of residue 24 resulted in marked changes in folding properites, suggesting the importance of this residue in folding of this protein.
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