Source:http://linkedlifedata.com/resource/pubmed/id/16737218
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2006-6-1
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pubmed:abstractText |
The rupture forces between an aptamer (1)-functionalized AFM tip and a thrombin-modified Au surface are analyzed. The rupture force for a single aptamer/thrombin complex is determined as approximately 4.45 pN. The analysis of the system reveals that the rupture forces correspond to the melting of the G-quadruplex structure of the aptamer bound to the thrombin. This melting of the G-quadruplex leads to the dissociation of the aptamer/thrombin complex.
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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:month |
Jun
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pubmed:issn |
0003-2700
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3638-42
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pubmed:meshHeading |
pubmed-meshheading:16737218-Aptamers, Nucleotide,
pubmed-meshheading:16737218-Base Sequence,
pubmed-meshheading:16737218-Gold,
pubmed-meshheading:16737218-Hydrogen Bonding,
pubmed-meshheading:16737218-Microscopy, Atomic Force,
pubmed-meshheading:16737218-Molecular Sequence Data,
pubmed-meshheading:16737218-Nucleic Acid Denaturation,
pubmed-meshheading:16737218-Stress, Mechanical,
pubmed-meshheading:16737218-Thrombin
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pubmed:year |
2006
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pubmed:articleTitle |
Following aptamer-thrombin binding by force measurements.
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pubmed:affiliation |
Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.
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pubmed:publicationType |
Journal Article
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