| pubmed-article:70038 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:70038 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:70038 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
| pubmed-article:70038 | lifeskim:mentions | umls-concept:C0023768 | lld:lifeskim |
| pubmed-article:70038 | lifeskim:mentions | umls-concept:C0012632 | lld:lifeskim |
| pubmed-article:70038 | lifeskim:mentions | umls-concept:C0596482 | lld:lifeskim |
| pubmed-article:70038 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:70038 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:70038 | lifeskim:mentions | umls-concept:C0018157 | lld:lifeskim |
| pubmed-article:70038 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:70038 | pubmed:dateCreated | 1977-9-22 | lld:pubmed |
| pubmed-article:70038 | pubmed:abstractText | Measurements with different chemically modified gramicidins in lipid bilayer membranes were used to discriminate between the dimeric pi(L,D) helix proposed by Urry and the dimeric parallel or antiparallel helices proposed by Veatch and Blout. Evidence for the pi(L,D) helix was obtained on the basis of the different actions of a negatively charged O-pyromellitylgramicidin and a negatively charged N-pyromellityldesformylgramicidin on lipid bilayer membranes. O-Pyromellitylgramicidin forms ionic channels in lipid membranes when it is applied to both sides of the membrane. In contrast to unmodified gramicidin, O-pyromellitylgramicidin is inactive when it is applied only to one side of the membrane. N-Pyromellityldesformylgramicidin does not form ionic channels in lipid bilayer membranes whether it is applied to one or both sides of the membrane. These results support the view that the gramicidin channel is formed by two pi(L,D) helices. Dimer formation by head-to-head association of two pi(L,D) helices needs six intermolecular hydrogen bonds, which are located at the formyl end of the molecule and which occur deep within the lipid membrane. In the head-to-head associated pi(L,D) helix the absence of the formyl group leads to an inactivation of the peptide, whereas in a parallel or antiparallel double-stranded helix the absence of the formyl group should have only minor effects. | lld:pubmed |
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| pubmed-article:70038 | pubmed:language | eng | lld:pubmed |
| pubmed-article:70038 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:70038 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:70038 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:70038 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:70038 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:70038 | pubmed:author | pubmed-author:BambergEE | lld:pubmed |
| pubmed-article:70038 | pubmed:author | pubmed-author:AlpesHH | lld:pubmed |
| pubmed-article:70038 | pubmed:author | pubmed-author:ApellH JHJ | lld:pubmed |
| pubmed-article:70038 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:70038 | pubmed:volume | 74 | lld:pubmed |
| pubmed-article:70038 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:70038 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:70038 | pubmed:pagination | 2402-6 | lld:pubmed |
| pubmed-article:70038 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:70038 | pubmed:meshHeading | pubmed-meshheading:70038-Gr... | lld:pubmed |
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| pubmed-article:70038 | pubmed:meshHeading | pubmed-meshheading:70038-El... | lld:pubmed |
| pubmed-article:70038 | pubmed:year | 1977 | lld:pubmed |
| pubmed-article:70038 | pubmed:articleTitle | Structure of the gramicidin A channel: discrimination between the piL,D and the beta helix by electrical measurements with lipid bilayer membranes. | lld:pubmed |
| pubmed-article:70038 | pubmed:publicationType | Journal Article | lld:pubmed |
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