Reconstitution of the acetylcholine receptor-channel system in planar bilayer membranes below lipid phase transition

1980 ◽  
Vol 6 (S1) ◽  
pp. 135-135
Author(s):  
G. Boheim ◽  
W. Hanke ◽  
F. J. Barrantes ◽  
H. Eibl ◽  
B. Sakmann ◽  
...  
Keyword(s):  
Phase Transition ◽  
Acetylcholine Receptor ◽  
Lipid Phase ◽  
Planar Bilayer ◽  
Lipid Phase Transition ◽  
Channel System ◽  
Bilayer Membranes ◽  
Acetylcholine Receptor Channel ◽  
Receptor Channel

Determination of Lipid Phase Transition Temperatures in Hybrid Bilayer Membranes

Langmuir ◽  
2006 ◽  
Vol 22 (20) ◽  
pp. 8333-8336 ◽  
Author(s):  
Neil A. Anderson ◽  
Lee J. Richter ◽  
John C. Stephenson ◽  
Kimberly A. Briggman
Keyword(s):  
Phase Transition ◽  
Lipid Phase ◽  
Transition Temperatures ◽  
Lipid Phase Transition ◽  
Bilayer Membranes ◽  
Phase Transition Temperatures ◽  
Hybrid Bilayer Membranes

Fatty acyl chain structure, orientational order, and the lipid phase transition in Acholeplasma laidlawii B membranes. A review of recent 19F nuclear magnetic resonance studies

1984 ◽  
Vol 62 (11) ◽  
pp. 1134-1150 ◽  
Author(s):  
P. M. Macdonald ◽  
B. D. Sykes ◽  
R. N. McElhaney
Keyword(s):  
Phase Transition ◽  
Fatty Acids ◽  
Nuclear Magnetic Resonance ◽  
Acyl Chain ◽  
Orientational Order ◽  
Membrane Lipid ◽  
Fatty Acyl ◽  
Fatty Acyl Chain ◽  
Lipid Phase ◽  
Lipid Phase Transition

The orientational order parameters of monofluoropalmitic acids biosynthetically incorporated into membranes of Acholeplasma laidlawii B in the presence of a large excess of a variety of structurally diverse fatty acids have been determined via 19F nuclear magnetic resonance (19F NMR) spectroscopy. It is demonstrated that these monofluoropalmitic acids are relatively nonperturbing membrane probes based upon physical (differential scanning calorimetry), biochemical (membrane lipid analysis), and biological (growth studies) criteria. 19F NMR is shown to convey the same qualitative and quantitative picture of membrane lipid order provided by 2H-NMR techniques and to be sensitive to the structural characteristics of the membrane fatty acyl chains, as well as to the lipid phase transition. Representatives of each naturally occurring class of fatty acyl chain structures, including straight-chain saturated, methyl-branched, monounsaturated, and alicyclic-ring-substituted fatty acids, were studied and the 19F-NMR order parameters were correlated with the lipid phase transitions (determined calorimetrically). The lipid phase transition was the prime determinant of overall orientational order regardless of fatty acid structure. Effects upon orientational order attributable to specific structural substituents were discernible, but were secondary to the effects of the lipid phase transition. In the gel state, relative overall order was directly proportional to the temperature of the particular lipid phase transition. Not only the overall order, but also the order profile across the membrane was sensitive to the presence of particular structural substituents. In particular, in the gel state specific fatty acyl structures demonstrated a characteristic disordering effect in the membrane order profile. These various observations can be merged to provide a unified picture of the manner in which fatty acyl chain chemistry modulates the physical state of membrane lipids.

The incorporation of cholesterol into inner mitochondrial membranes and its effect on lipid phase transition

1980 ◽  
Vol 599 (2) ◽  
pp. 528-537 ◽  
Author(s):  
Thomas D. Madden ◽  
Carmen Vigo ◽  
K.Richard Bruckdorfer ◽  
Dennis Chapman
Keyword(s):  
Phase Transition ◽  
Lipid Phase ◽  
Mitochondrial Membranes ◽  
Lipid Phase Transition

Stratified organization of the nicotinic acetylcholine receptor channel

Neuroreport ◽  
1992 ◽  
Vol 3 (11) ◽  
pp. 1001-1004 ◽  
Author(s):  
A. Devillérs-Thiery ◽  
J. L. Galzi ◽  
S. Bertrand ◽  
J. P. Changeux ◽  
D. Bertrand
Keyword(s):  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Nicotinic Acetylcholine ◽  
Acetylcholine Receptor Channel ◽  
Receptor Channel
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