Average membrane penetration depth of tryptophan residues of the nicotinic acetylcholine receptor by the parallax method.

@article{Chattopadhyay1991AverageMP,
  title={Average membrane penetration depth of tryptophan residues of the nicotinic acetylcholine receptor by the parallax method.},
  author={Amitabha Chattopadhyay and Mark G. McNamee},
  journal={Biochemistry},
  year={1991},
  volume={30 29},
  pages={
          7159-64
        }
}
The membrane penetration depths of tryptophan residues in the nicotinic acetylcholine receptor from Torpedo californica have been analyzed in reconstituted membranes containing purified receptor and defined lipids. Dioleoylphosphatidylcholine and three spin-labeled phosphatidylcholines with the nitroxide group at three different positions on the fatty acyl chain were used for reconstitution of the receptor. The spin-labeled phospholipids serve as quenchers of tryptophan fluorescence… 
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Calibration of the parallax fluorescence quenching method for determination of membrane penetration depth: refinement and comparison of quenching by spin-labeled and brominated lipids.
TLDR
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References

SHOWING 1-10 OF 50 REFERENCES
Tryptophan imaging of membrane proteins.
TLDR
It is shown that even for cases in which little is known about the quantum yield distribution, significant information can be determined about the tryptophan spatial distribution.
Annular and nonannular binding sites for cholesterol associated with the nicotinic acetylcholine receptor.
TLDR
Interactions between lipids and the nicotinic acetylcholine receptor from Torpedo californica have been measured in reconstituted membranes containing purified receptor and defined lipids, and analysis of the quenching data suggests that there are 5-10 nonannular sites associated with the receptor.
Location of tryptophans in membrane-bound annexins.
  • P. Meers
  • Chemistry, Medicine
    Biochemistry
  • 1990
TLDR
The annexins are a novel class of calcium-dependent membrane binding proteins with highly homologous sequences and similar binding characteristics and data on the bovine liver calelectrins is presented showing that endonexin also has a tryptophan residue that interacts strongly with phospholipids.
Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids.
TLDR
The method involves determination of the parallax in the apparent location of fluorophores detected when quenching by phospholipids spin-labeled at two different depths and it is shown that the calculated depths of the NBD groups are self-consistent no matter which two spin-labels have been used in a particular experiment.
A minimum number of lipids are required to support the functional properties of the nicotinic acetylcholine receptor.
TLDR
The detergent sodium cholate was used to both solubilize and partially delipidate the nicotinic acetylcholine receptor from Torpedo californica and revealed that a minimum of 45 lipids per receptor was required for stabilization of the receptor in a fully functional state.
Immobilized lipid in acetylcholine receptor-rich membranes from Torpedo marmorata.
  • D. Marsh, F. Barrantes
  • Chemistry, Medicine
    Proceedings of the National Academy of Sciences of the United States of America
  • 1978
TLDR
The lipid environment of acetylcholine receptor-rich membranes from Torpedo marmorata has been studied with spin labels and shows that the protein-associated lipid is immobilized with respect to rotation both around and perpendicular to the long molecular axis.
Agonist-mediated changes of the acetylcholine receptor in its membrane environment.
  • F. Barrantes
  • Chemistry, Medicine
    Journal of molecular biology
  • 1978
TLDR
The interaction of a cholinergic agonist, suberyldicholine, with the membrane-bound acetylcholine receptor from Torpedo marmorata was studied in vitro by a combination of kinetic and steady-state techniques, and the final, “high-affinity” state of the complex is tentatively attributed to the “desensitised” conformation postulated from in vivo studies.
Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor.
TLDR
The lipids having the highest affinity for the acetylcholine receptor were also those that have the largest effects on the ion flux functional properties of the receptor, and the results are discussed in terms of lipid effects on receptor function.
Inhibition of ion permeability control properties of acetylcholine receptor from Torpedo californica by long-chain fatty acids.
TLDR
The effects of free fatty acids on acetylcholine receptor function are attributed to the disruptions of protein-lipid interactions.
Correlation between acetylcholine receptor function and structural properties of membranes.
TLDR
It was found that both aspects of AChR function were highly dependent on the lipid environment even though carbamylcholine binding itself was not affected, and an appropriate membrane fluidity was necessarily required to allow the interconversion between the low and high affinity states of A ChR.
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