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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1995-4-20
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pubmed:abstractText |
In an effort to understand the molecular mechanisms of voltage activation of ion channels, we have chosen a system of known structure and examined the properties of heterodimeric channels formed between [Val1]gramicidin A ([Val1]gA) and [F6Val1]gramicidin A ([F6Val1]gA). Gramicidin channels are usually not voltage-dependent; but the introduction of a single symmetry-breaking dipolar F6Val1 residue into a ([Val1]gA)2 dimer to form the [F6Val1]gA/[Val1]gA heterodimer induces voltage-dependent transitions between two conducting states: a high-conductance state and a zero conductance (closed) state. The distribution between these states varies as a function of the applied potential but is not dependent on the nature of the permeant ion (H+ or Cs+). The permeating ions do not seem to contribute to the apparent gating charge.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-1280467,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-1376169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-1553560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-1688951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-1689177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-1700867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-1721242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-1846229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-2414241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-2421794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-2543931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-5276779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-666725,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-7521224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-7682046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-7690158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7534411-81687
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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 |
Mar
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
92
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2121-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7534411-Calcium Channels,
pubmed-meshheading:7534411-Cesium,
pubmed-meshheading:7534411-Gramicidin,
pubmed-meshheading:7534411-Ion Channel Gating,
pubmed-meshheading:7534411-Ion Channels,
pubmed-meshheading:7534411-Kinetics,
pubmed-meshheading:7534411-Lipid Bilayers,
pubmed-meshheading:7534411-Macromolecular Substances,
pubmed-meshheading:7534411-Membrane Potentials,
pubmed-meshheading:7534411-Models, Biological,
pubmed-meshheading:7534411-Structure-Activity Relationship,
pubmed-meshheading:7534411-Valine
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pubmed:year |
1995
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pubmed:articleTitle |
Voltage-dependent gating of an asymmetric gramicidin channel.
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pubmed:affiliation |
Department of Physiology and Biophysics, Cornell University Medical College, New York, NY 10021.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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