Molecular dynamics study of the LS3 voltage‐gated ion channel
Open Access
- 8 May 1998
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 427 (2) , 267-270
- https://doi.org/10.1016/s0014-5793(98)00304-4
Abstract
Molecular dynamics calculations have been carried out on a model of the LS3 synthetic ion channel in a membrane mimetic environment. In the absence of an external electrostatic field, the LS3 channel, which consists of a bundle of six α‐helices with sequence Ac‐(LSSLLSL)3‐CONH2, exhibits large structural fluctuations. However, in the presence of the field, the bundle adopts a well defined coiled‐coil structure with an inner pore of water. The observed structural changes induced by the applied field are consistent with the proposed gating mechanism of the ion channel.Keywords
This publication has 22 references indexed in Scilit:
- Charge selectivity of the designed uncharged peptide ion channel Ac-(LSSLLSL)3-CONH2Biophysical Journal, 1995
- A helical-dipole model describes the single-channel current rectification of an uncharged peptide ion channel.Proceedings of the National Academy of Sciences, 1994
- Synthetic peptides as models for ion channel proteinsAccounts of Chemical Research, 1993
- Fluorescence studies of the secondary structure and orientation of a model ion channel peptide in phospholipid vesiclesBiochemistry, 1992
- Contribution of theoretical chemistry to the study of ion transport through membranesChemical Reviews, 1991
- Ion transport in a model gramicidin channel. Structure and thermodynamicsBiophysical Journal, 1991
- Bundles of amphipathic transmembrane α‐helices as a structural motif for ion‐conducting channel proteins: Studies on sodium channels and acetylcholine receptorsProteins-Structure Function and Bioinformatics, 1990
- M2 delta, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor.Proceedings of the National Academy of Sciences, 1988
- Synthetic Amphiphilic Peptide Models for Protein Ion ChannelsScience, 1988
- Channel protein engineering: synthetic 22-mer peptide from the primary structure of the voltage-sensitive sodium channel forms ionic channels in lipid bilayers.Proceedings of the National Academy of Sciences, 1988