APOMYOGLOBIN에 의한 MICELLE화 과정의 작용모델 = WORKING MODEL OF MICELLIZATION INDUCED BY APOMYOGLOBIN

다국어 초록 (Multilingual Abstract)

Abstract. Many studies for micellization by proteins have been reported and it's working models have been suggested. Also, structure of apomyoglobin has been very much studied and many informations are useful now. From all these data and results in this paper that is experimental and theoretical, a new working model for micellization is proposed. Five amphiphilic α-helices (A, B, E, Ii and G helices) of apomyoglobin predicted by hydrophobic moment plot may interact with phospholipids. The E helix of these that is very hydrophobic may initially interact with phospholipid and then others may bind at the surface of bilayer. The F helix may penetrate deeply into the lipid bilayer with dragging other helices. As the apomyoglobins were more bound to the vesicles, the polar faces of these helices may aggregate to form pore in the membrane. Finally the polar face of these amphiphilic a-helix may be exposed to aqueous phase and the vesicle may be broken down into micellar forms.