Stability and folding of a mutant ribose binding protein of escherichia coli = 대장균의 돌연변이 리보스 결합 단백질의 안정성 및 폴딩에 관한 연구

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A mature mutant ribose binding protein (RBP) of Escherichia coli was obtained by site-directed mutagenesis, replacing Thr-3 in the N-domain of wild-type mature RBP (WT-mRBP) with a Trp residue (N-Trp-mRBP). The equilibrium unfolding properties and the refolding kinetics of this protein were monitored by fluorescence and circular dichroism (CD). The stability of N-Trp-mRBP appears to be the same as that of C-Trp-mRBP, another mutant obtained by relpacing Phe-187 with a Trp, and lower than that of WT-mRBP. The overall refolding rate of N-Trp-mRBP was much smaller than that of C-Trp-mRBP which ,in turn, is similar to that of WT-mRBP. For the case of WT-mRBP, the rate constant obtained by Tyr fluorescence was identical to the value obtained by CD. But with C-Trp- mRBP, the rate constant from CD was smaller than the value from the Trp- fluorescence and this difference in the rate constants was much greater with the N-Trp-mRBP.
Advisors
Kim, Hyoung-Man김형만
Description
한국과학기술원 : 생물과학과,
Publisher
한국과학기술원
Issue Date
1997
Identifier
112651/325007 / 000953120
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생물과학과, 1997.2, [ vi, 48 p. ]

Keywords

리폴딩 키네틱스; 평형 언폴딩; 도메인 폴딩; Mutant ribose binding protein; Equilibrium unfolding; Refolding kinetics; Domain folding; 리보스 결합 단백질

URI
http://hdl.handle.net/10203/28514
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=112651&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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