Structural studies on the signal sequence of E.coli ribose-binding protein by CD = CD 방법에 의한 대장균 리보스결합 단백질내 신호서열의 구조에 관한 연구

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The structures of chemically synthesized funtional and nonfunctional signal peptides of Escherichia coli ribose binding protein were determined by CD in trifluoroethanol solution which mimmics the amphiphilic environment. The estimated value of helix content of the wild type was found to be 98\% at 25$^\circ$C and 86\% 50$^\circ$C. The estimated $\alpha$-helix content of the mutant peptide was 55\% at 25$^\circ$C and less than 10\% at 50$^\circ$C. It appeared that the Pro-9 residue in nonfunctional peptide disturbs the helix. Sine the $\alpha$-helix segment of the wild type signal peptide is longer than that of the mutant signal sequence, it appears that the necessary condition for the translocation of RBP is the dimension of the helix in the signal sequence.
Advisors
Kim, Hyoung-Man김형만
Description
한국과학기술원 : 생명과학과,
Publisher
한국과학기술원
Issue Date
1993
Identifier
68319/325007 / 000911561
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생명과학과, 1993.2, [ v, 39 p. ]

URI
http://hdl.handle.net/10203/28407
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=68319&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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