Structural studies of peptide hormone and signal sequence of escherichia coli ribose binding protein by NMR = NMR 방법에 의한 펩티드 호르몬과 대장균 리보스 결합 단백질내 신호서열의 구조 연구

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The structures of two peptide hormones, glucagon and luteinizing hormone releasing hormone, and functional and non-functional signal peptides of Escherichia coli ribose binding protein have been elucidated by detailed NMR and CD. The results are summarized below. (1) The structure of monomeric glucagon in dilute aqueous solution was studied by 500 MHz NMR. Hydrogen-deuterium exchange experiments monitored by NMR showed that the backbone amide NHs form intrastrand hydrogen bonds suggesting the existence of some degree of compact structure. The temperature dependent shift of several amide NH resonances supported the above conclusion. The small J coupling constants arising from the interactions between 6 amide NHs and C$\alpha$Hs(less than 6 Hz) implied a helical structure. (2) The NMR and CD studies on the structure of LHRH in water/TFE solution were performed at pH 3 and pH 7. At pH 3, no discernible structure was seen by CD measurement in the temperatures of 10$^\circ$C and 25$^\circ$C. But the evidences of the existence of a turn was obtained by NMR measurement at 10$\circ$C. At pH 5, and in more higher pH, the preference of $\beta$-structure was found. The effect of pH on the LHRH structure was discussed. In addition of $\beta$-structure, we could find out the characteristic NOEs of $\beta$-turn at pH 7. It seems that the antiparallel $\beta$-structure accompanying $\beta$-turn on the middle of sequence is unstable at low pH due to the ionization of His-2 residue. We suggest that the main structures of LHRH are $\beta$-turn and $\beta$-structure in water/TFE solution and there is an unusual turn rather than the random structure at low pH, water/TFE(1:1 by volume) solution. (3) The structures of chemically synthesized functional and non-functional signal peptides of Escherichia coli ribose binding protein were compared in the solvents which mimic the amphiphilic environments by CD and 2D 1H NMR. The functional peptide have a helix consisted of 19 residues star...
Advisors
Kim, Hyoung-ManChoi, Byong-Seok김형만최병석
Description
한국과학기술원 : 생명과학과,
Publisher
한국과학기술원
Issue Date
1993
Identifier
60613/325007 / 000885317
Language
eng
Description

학위논문(박사) - 한국과학기술원 : 생명과학과, 1993.2, [ vi, 128 p. ]

Keywords

황체 형성 호르몬 분비 호르몬.

URI
http://hdl.handle.net/10203/27334
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=60613&flag=dissertation
Appears in Collection
BS-Theses_Ph.D.(박사논문)
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