3P126 Thermalstability of bacteriorhodopsin reconstituted in DMPC liposome
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منابع مشابه
The photochemical reaction cycle of retinal reconstituted bacteriorhodopsin.
The function of three types of bacteriorhodopsins was compared: the wild-type, the bleached and retinal reconstituted and retinal deficient bacteriorhodopsin after retinal addition. The apparent pK(a) of the proton acceptor group for the bleached BR and retinal deficient BR shifted toward higher pH values compared to the wild-type BR. Fitting the photocycle model to the absorption kinetic signa...
متن کاملMonomer-oligomer equilibrium of bacteriorhodopsin in reconstituted proteoliposomes. A freeze-fracture electron microscope study.
An improved freeze-fracture electron microscope procedure has been developed and applied to the study of the association of bacteriorhodopsin in large proteoliposomes reconstituted by reverse-phase evaporation with egg lecithin. Due to the improved accuracy and resolution of this procedure, intramembrane particles, the diameter of which (4.5 nm) closely matched that of bacteriorhodopsin monomer...
متن کاملEffect of membrane potential on the conformation of bacteriorhodopsin reconstituted in lipid vesicles.
The effect of applied diffusion potential on circular dichroism (CD) of bacteriorhodopsin, reconstituted in lipid vesicles, was measured. The change in CD indicates that the applied electrical field, irrespective of its direction, decreases the alpha-helical fraction and increases the random fraction of the protein. The results are interpreted by unfolding of edges of the helices, upon their su...
متن کامل[Preparation of liposome containing bacteriorhodopsin with natural preferred orientation of its transient photoresponse].
Bacteriorhodopsin is a membrane protein of halobacteria and functions as a light-driven protein pump. After we isolated bR from cultured halobacteria, bR was mixed with amphiphilic DPPC under different pH. The liposomes were formed after sonication. The remaining biological activity of bR as a proton pump was then verified and pulsed-light-induced proton movement was detected, while liposomes w...
متن کاملThe low-resolution structure of nHDL reconstituted with DMPC with and without cholesterol reveals a mechanism for particle expansion.
Small-angle neutron scattering (SANS) with contrast variation was used to obtain the low-resolution structure of nascent HDL (nHDL) reconstituted with dimyristoyl phosphatidylcholine (DMPC) in the absence and presence of cholesterol, [apoA1:DMPC (1:80, mol:mol) and apoA1:DMPC:cholesterol (1:86:9, mol:mol:mol)]. The overall shape of both particles is discoidal with the low-resolution structure o...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2005
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.45.s235_2