A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution

@article{Fox1982AVI,
  title={A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution},
  author={Robert O. Fox and Frederic M. Richards},
  journal={Nature},
  year={1982},
  volume={300},
  pages={325-330}
}
The crystal structure of alamethicin in nonaqueous solvent has been determined, and refined at 1.5-Å resolution. The molecular conformation of the three crystallographically independent molecules is largely α-helical with a bend in the helix axis at an internal proline residue. The helix structure is highly amphipathic as most of the solvent-accessible polar atoms lie on a narrow strip of surface parallel to the helix axis. Molecular models for the voltage-gated ion channel, with n-fold… 
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The Effects of Environment on the Conformation of the Alamethicin Membrane Channel a
TLDR
Circular dichroism (CD) spectroscopy has been used in this study to compare the secondary structure of alamethicin in membranes and in the solvent system from which the crystals were formed.
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Crystals of an ion-channel-forming peptaibol peptide in a partial membrane environment have been obtained by cocrystallizing antiamoebin with n-octanol. The antiamoebin molecule has a bent helical…
The mechanism of channel formation by alamethicin as viewed by molecular dynamics simulations.
TLDR
Molecular dynamics simulations of alamethicin in a number of different environments have been used to explore its channel-forming properties and provide a set of dynamic snapshots of a possible mechanism of channel formation by this peptide.
Conformational study of a synthetic analogue of alamethicin. Influence of the conformation on ion-channel lifetimes.
TLDR
A conformational study of L2 was undertaken using FTIR, CD and NMR spectroscopy, and the secondary structure showed an enhanced predominant helical structure as compared to alamethicin, resulting in a smaller length of the L2 peptide.
Solution NMR studies of antiamoebin, a membrane channel-forming polypeptide.
THE STRUCTURE AND DYNAMICS OF MEMBRANE SPANNING HELICES BY HIGH RESOLUTION NMR AND MOLECULAR DYNAMICS
High resolution 1H NMR can now be used to determine the structure of proteins in solution. Using this method, detailed structures of three helix forming peptides have been determined in organic…
Implicit solvent model estimates of the stability of model structures of the alamethicin channel
TLDR
Analysis of the results suggests two causes for the apparent instability of the remainder of the structures inside the lipid bilayer, both resulting from the desolvation of channel polar groups (i.e. their transfer from the aqueous phase into the bilayer) and the apparent conflict between continuum-solvent and MD calculations.
Alamethicin channels in a membrane: molecular dynamics simulations.
TLDR
These simulations explore the stability and conformational dynamics of these helix bundle channels when embedded in a full phospholipid bilayer in an aqueous environment and the structural and dynamic properties of water in these model channels are examined.
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References

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TLDR
The voltage-dependent gating displays all the characteristics observed in excitable cells and its basic features can be quantitatively described by the Hodgkin-Huxley equations.
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TLDR
It is proposed that the conducting complex is capable of functioning in either of two orientations, and that it is these two possibilities that give rise to certain differences in the single channel characteristics for the two directions of the field.
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TLDR
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