Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
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Unfolding Property of Residue 24-Substituted Tryptophan Synthase $\alpha$-Subunits

24번 잔기가 치환된 트립토판 중합효소 $\alpha$ 소단위체들의 구조풀림 성질

  • 정지은 (부산대학교 자연과학대학 분자생물학과) ;
  • 박후휘 (부산대학교 자연과학대학 분자생물학과) ;
  • 신혜자 (동서대학교 환경공학과) ;
  • 임운기 (부산대학교 자연과학대학 분자생물학과)
  • Published : 1999.12.01
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Abstract

The doubly altered mutant tryptophan synthase $\alpha$-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.

대장균 트립토판 중합요소 (tryptophan synthase) $\alpha$ 소단위체의 24번 잔기인 트레오닌이 메티오닌, 알라닌 또는 세린으로 치환되고 잔기 139에 트립토판이 있는 단백질를 정제하여, 여러가지 요소 농도에 대한 트립토판 형광값의 변화를 측정하여 변성곡선을 얻었다. 이들 단백질들은 모두 F139W 단백질에 비해 구조형성 성질에 큰 변화를 일으켰으며, 잔기 24번은 구조형성에 중요한 것으로 추정된다.

Keywords

References

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