Formation of the micellar complex by apomyoglobin = Apomyoglobin 에 의한 micellar complex 의 형성에 관한 연구

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Amphipathic helices have been regarded as the basic lipid-associating domains of micellar complex formation. Apomyoglobin has still 27% α-helix at pH 4, and most of these helices are amphipathic. As the model system, the interaction between apomyoglobin and dimyristoylphosphatidylcholine (DMPC) is studied. At pH 4 and low lipid/protein molar ratio, the size decrease of DMPC vesicle is identified by light-scattering and Sepharose CL-4B column chromatography. The shape of vesicle-protein complex is observed to be changed from sphere to cigar form by electron-microscopic study. From the quenching test of tryptophan, it seems that N-terminal region of apomyoglobin is hydrophobically participated.
Advisors
Rhee, Joon-Shick이준식
Description
한국과학기술원 : 생물공학과,
Publisher
한국과학기술원
Issue Date
1988
Identifier
66136/325007 / 000861337
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생물공학과, 1988.2, [ vi, 41 p. ]

URI
http://hdl.handle.net/10203/28294
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=66136&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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