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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2 Pt 1
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pubmed:dateCreated |
1997-6-6
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pubmed:abstractText |
Alamethicin is an alpha-helical peptide that forms voltage-activated ion channels. Experimental data suggest that channel formation occurs via voltage-dependent insertion of alamethicin helices into lipid bilayers, followed by self-assembly of inserted helices to form a parallel helix bundle. Changes in the kink angle of the alamethicin helix about its central proline residue have also been suggested to play a role in channel gating. Alamethicin helices generated by simulated annealing and restrained molecular dynamics adopt a kink angle similar to that in the x-ray crystal structure, even if such simulations start with an idealized unkinked helix. This suggests that the kinked helix represents a stable conformation of the molecule. Molecular dynamics simulations in the presence of a simple bilayer model and a transbilayer voltage difference are used to explore possible mechanisms of helix insertion. The bilayer is represented by a hydrophobicity potential. An alamethicin helix inserts spontaneously in the absence of a transbilayer voltage. Application of a cis positive voltage decreases the time to insertion. The helix kink angle fluctuates during the simulations. Insertion of the helix is associated with a decrease in the mean kink angle, thus helping the alamethicin molecule to span the bilayer. The simulation results are discussed in terms of models of alamethicin channel gating.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-1279177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-1507229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-1692484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-19431805,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-1946322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-2081267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-2424473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-2436657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-2924737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-3207847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-3663608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-427100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-4461846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-6292726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-6324906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-6385134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7488617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7495788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7520180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7522664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7525266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7529585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7532020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7602600,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7626742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7627551,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7756540,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7766829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7800037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7849226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-7947910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8218891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8369434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8441750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8445638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8451235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8534808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8555220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8599639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8599645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8628736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8637016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8639562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8679929,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8785337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8785340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8837517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-8889144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9017192-9005437
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
72
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
627-36
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:9017192-Alamethicin,
pubmed-meshheading:9017192-Amino Acid Sequence,
pubmed-meshheading:9017192-Chemistry, Physical,
pubmed-meshheading:9017192-Computer Simulation,
pubmed-meshheading:9017192-Crystallography, X-Ray,
pubmed-meshheading:9017192-Ion Channel Gating,
pubmed-meshheading:9017192-Ion Channels,
pubmed-meshheading:9017192-Lipid Bilayers,
pubmed-meshheading:9017192-Membrane Potentials,
pubmed-meshheading:9017192-Models, Molecular,
pubmed-meshheading:9017192-Molecular Sequence Data,
pubmed-meshheading:9017192-Physicochemical Phenomena,
pubmed-meshheading:9017192-Protein Conformation,
pubmed-meshheading:9017192-Protein Structure, Secondary
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pubmed:year |
1997
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pubmed:articleTitle |
Simulation studies of alamethicin-bilayer interactions.
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pubmed:affiliation |
Laboratory of Molecular Biophysics, University of Oxford, England.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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