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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1995-10-4
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pubmed:abstractText |
The effect of anionic lipids on the membrane insertion of a carboxyl group on a specially designed palmitoylated peptide was studied, using tryptophan fluorescence. It is demonstrated that the negatively charged membrane surface of mixed phosphatidylcholine/phosphatidylglycerol small unilamellar vesicles enhances the protonation of the C-terminal carboxyl group, and the subsequent insertion of that part of the peptide.
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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 |
Aug
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
370
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
189-92
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7656974-Amino Acid Sequence,
pubmed-meshheading:7656974-Anions,
pubmed-meshheading:7656974-Arginine,
pubmed-meshheading:7656974-Buffers,
pubmed-meshheading:7656974-Hydrogen-Ion Concentration,
pubmed-meshheading:7656974-Lipid Bilayers,
pubmed-meshheading:7656974-Membrane Proteins,
pubmed-meshheading:7656974-Molecular Sequence Data,
pubmed-meshheading:7656974-Peptides,
pubmed-meshheading:7656974-Phospholipids,
pubmed-meshheading:7656974-Protons,
pubmed-meshheading:7656974-Spectrometry, Fluorescence,
pubmed-meshheading:7656974-Surface Properties,
pubmed-meshheading:7656974-Tryptophan
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pubmed:year |
1995
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pubmed:articleTitle |
Anionic phospholipids can mediate membrane insertion of the anionic part of a bound peptide.
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pubmed:affiliation |
Department of Biochemistry of Membranes (CBLE), Utrecht University, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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