pubmed-article:2172017 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2172017 | lifeskim:mentions | umls-concept:C0023768 | lld:lifeskim |
pubmed-article:2172017 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
pubmed-article:2172017 | lifeskim:mentions | umls-concept:C0162807 | lld:lifeskim |
pubmed-article:2172017 | lifeskim:mentions | umls-concept:C0037081 | lld:lifeskim |
pubmed-article:2172017 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:2172017 | pubmed:dateCreated | 1990-12-13 | lld:pubmed |
pubmed-article:2172017 | pubmed:abstractText | The secondary structure of the synthetic signal peptide of cytochrome c oxidase subunit IV (coxIV-25) has been measured by circular dichroism spectroscopy in different lipid environments. CoxIV-25 is polymorphic in membranes. It forms an amphiphilic alpha-helix both in negatively charged lipid bilayers (up to 49% helix) and in detergent micelles (up to 42% helix). In association with bilayers of the zwitterionic lipid phosphatidylcholine, coxIV-25 takes an aperiodic, unidentified structure. CoxIV-25 is also partially alpha-helical in bilayers of cardiolipin, mitochondrial lipid extracts and mixtures of synthetic phosphatidylcholine and phosphatidylglycerol. | lld:pubmed |
pubmed-article:2172017 | pubmed:language | eng | lld:pubmed |
pubmed-article:2172017 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2172017 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2172017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2172017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2172017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2172017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2172017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2172017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2172017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2172017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2172017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2172017 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2172017 | pubmed:month | Oct | lld:pubmed |
pubmed-article:2172017 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:2172017 | pubmed:author | pubmed-author:TammL KLK | lld:pubmed |
pubmed-article:2172017 | pubmed:author | pubmed-author:BartoldusII | lld:pubmed |
pubmed-article:2172017 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2172017 | pubmed:day | 15 | lld:pubmed |
pubmed-article:2172017 | pubmed:volume | 272 | lld:pubmed |
pubmed-article:2172017 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2172017 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2172017 | pubmed:pagination | 29-33 | lld:pubmed |
pubmed-article:2172017 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:2172017 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2172017 | pubmed:articleTitle | Secondary structure of a mitochondrial signal peptide in lipid bilayer membranes. | lld:pubmed |
pubmed-article:2172017 | pubmed:affiliation | Department of Biophysical Chemistry, University of Basel, Switzerland. | lld:pubmed |
pubmed-article:2172017 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2172017 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:2172017 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2172017 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2172017 | lld:pubmed |