Source:http://linkedlifedata.com/resource/pubmed/id/11433211
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2001-7-3
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pubmed:abstractText |
The complexing of Congo red in two different ligand forms - unimolecular and supramolecular (seven molecules in a micelle) - with eight deca-peptides organized in a b-sheet was tested by computational analysis to identify its dye-binding preferences. Polyphenylananine and polylysine peptides were selected to represent the specific side chain interactions expected to ensure particularly the stabilization of the dye-protein complex. Polyalanine was used to verify the participation of non-specific backbone-derived interactions.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1234-1010
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
771-84
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading | |
pubmed:articleTitle |
Why Congo red binding is specific for amyloid proteins - model studies and a computer analysis approach.
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pubmed:affiliation |
Department of Biostatistics and Medical Informatics, Collegium Medicum, Jagiellonian University, Cracow, Poland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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