The effect of bacteriorhodopsin, detergent and hydration on the cubic-to-lamellar phase transition in the monoolein-distearoyl phosphatidyl glycerol-water system
(2004) In Biochimica et Biophysica Acta - Biomembranes 1665(1-2). p.156-166- Abstract
- The cubic phase of monoolein (MO) has successfully been used for crystallization of membrane proteins. It is likely that the transition to a lamellar phase upon dehydration is important for the crystallization process, and that the internal dimensions of the lipid phases (i.e., water pore diameter) are crucial for the inclusion and the diffusion of membrane proteins. In the present study, we investigated the cubic-to-lamellar phase transitions in the MO-water and the MO-distearoyl phosphatidyl glycerol (DSPG) systems. The MO-water system was investigated by means of isothermal sorption and desorption microcalorimetry. We show that the transition from cubic to lamellar phase induced by desorption is driven by entropy. At 25 degreesC, this... (More)
- The cubic phase of monoolein (MO) has successfully been used for crystallization of membrane proteins. It is likely that the transition to a lamellar phase upon dehydration is important for the crystallization process, and that the internal dimensions of the lipid phases (i.e., water pore diameter) are crucial for the inclusion and the diffusion of membrane proteins. In the present study, we investigated the cubic-to-lamellar phase transitions in the MO-water and the MO-distearoyl phosphatidyl glycerol (DSPG) systems. The MO-water system was investigated by means of isothermal sorption and desorption microcalorimetry. We show that the transition from cubic to lamellar phase induced by desorption is driven by entropy. At 25 degreesC, this occurs at a water activity of 0.98 with a transition enthalpy of 860 J/mol (MO). The phase behavior was also investigated in the presence of a small amount of the transmembrane protein bacteriorhodopsin (bR), and a detergent, octyl glucoside (OG), and it was shown that both bR and OG stabilize the lamellar phase. Analogous results were obtained for the MO-DSPG-water system. The latter system resembles the MO-water system in that a cubic-to-lamellar phase transition is induced by dehydration, although the structural properties of these phases are slightly different. Finally, we demonstrate that bR can be crystallized from a cubic phase of MO-DSPG-buffer. (C) 2004 Elsevier B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/154141
- author
- Sparr, Emma LU ; Wadsten, P ; Kocherbitov, Vitaly LU and Engström, S
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochimica et Biophysica Acta - Biomembranes
- volume
- 1665
- issue
- 1-2
- pages
- 156 - 166
- publisher
- Elsevier
- external identifiers
-
- pmid:15471581
- wos:000224462900017
- scopus:4644279591
- ISSN
- 0005-2736
- DOI
- 10.1016/j.bbamem.2004.07.005
- language
- English
- LU publication?
- yes
- id
- 1b1701f2-4048-46d2-898f-3acbdf4d28de (old id 154141)
- date added to LUP
- 2016-04-01 16:54:35
- date last changed
- 2022-04-07 19:32:25
@article{1b1701f2-4048-46d2-898f-3acbdf4d28de,
abstract = {{The cubic phase of monoolein (MO) has successfully been used for crystallization of membrane proteins. It is likely that the transition to a lamellar phase upon dehydration is important for the crystallization process, and that the internal dimensions of the lipid phases (i.e., water pore diameter) are crucial for the inclusion and the diffusion of membrane proteins. In the present study, we investigated the cubic-to-lamellar phase transitions in the MO-water and the MO-distearoyl phosphatidyl glycerol (DSPG) systems. The MO-water system was investigated by means of isothermal sorption and desorption microcalorimetry. We show that the transition from cubic to lamellar phase induced by desorption is driven by entropy. At 25 degreesC, this occurs at a water activity of 0.98 with a transition enthalpy of 860 J/mol (MO). The phase behavior was also investigated in the presence of a small amount of the transmembrane protein bacteriorhodopsin (bR), and a detergent, octyl glucoside (OG), and it was shown that both bR and OG stabilize the lamellar phase. Analogous results were obtained for the MO-DSPG-water system. The latter system resembles the MO-water system in that a cubic-to-lamellar phase transition is induced by dehydration, although the structural properties of these phases are slightly different. Finally, we demonstrate that bR can be crystallized from a cubic phase of MO-DSPG-buffer. (C) 2004 Elsevier B.V. All rights reserved.}},
author = {{Sparr, Emma and Wadsten, P and Kocherbitov, Vitaly and Engström, S}},
issn = {{0005-2736}},
language = {{eng}},
number = {{1-2}},
pages = {{156--166}},
publisher = {{Elsevier}},
series = {{Biochimica et Biophysica Acta - Biomembranes}},
title = {{The effect of bacteriorhodopsin, detergent and hydration on the cubic-to-lamellar phase transition in the monoolein-distearoyl phosphatidyl glycerol-water system}},
url = {{http://dx.doi.org/10.1016/j.bbamem.2004.07.005}},
doi = {{10.1016/j.bbamem.2004.07.005}},
volume = {{1665}},
year = {{2004}},
}