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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
2005-6-17
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pubmed:abstractText |
A histidine-coordinating metal complex substituted with methoxypyrrole amino acids (MOPAS) as a peptide beta-sheet binder shows high affinity for a H(2)N-His-Leu-Leu-Val-Phe-OMe pentapeptide in DMSO solution. Within the complex, a beta-sheet conformation is induced into the pentapeptide by weak intra-assembly interactions with the MOPAS units.
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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 |
Jun
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pubmed:issn |
0022-3263
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
70
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5305-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15960536-Amino Acid Sequence,
pubmed-meshheading:15960536-Amino Acids,
pubmed-meshheading:15960536-Ligands,
pubmed-meshheading:15960536-Models, Molecular,
pubmed-meshheading:15960536-Molecular Structure,
pubmed-meshheading:15960536-Oligopeptides,
pubmed-meshheading:15960536-Protein Conformation,
pubmed-meshheading:15960536-Protein Structure, Secondary,
pubmed-meshheading:15960536-Stereoisomerism
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pubmed:year |
2005
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pubmed:articleTitle |
Enhanced peptide beta-sheet affinity by metal to ligand coordination.
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pubmed:affiliation |
Institut für Organische Chemie, Universität Regensburg, Universitätsstrasse 31, D-93040 Regensburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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