rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
1992-6-29
|
pubmed:abstractText |
The contribution of different factors in the interaction of ethidium intercalated into various sequences of a triple helix, or in the region of the junction between the double- and triple-stranded DNA has been studied by energy minimization. It is found that in the total energy of the ethidium- triple helix complexes, a particular electrostatic contribution emerges due to the presence of protonated cytosines in the triple helix. This parameters is determinant in the sequence-specificity of ethidium binding to the triple helix. The preferred intercalation sites of ethidium in the triple helix are proposed. The interaction of ethidium at the triplex-duplex junction, and its effects are also discussed. This study is aimed at searching for new drugs specific for the triple helix, or for the triplex-duplex junctions.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0739-1102
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
9
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
425-436
|
pubmed:dateRevised |
2000-12-18
|
pubmed:meshHeading |
pubmed-meshheading:1815636-Base Sequence,
pubmed-meshheading:1815636-DNA,
pubmed-meshheading:1815636-Deoxyribonucleotides,
pubmed-meshheading:1815636-Ethidium,
pubmed-meshheading:1815636-Hydrogen Bonding,
pubmed-meshheading:1815636-Intercalating Agents,
pubmed-meshheading:1815636-Molecular Sequence Data,
pubmed-meshheading:1815636-Nucleic Acid Conformation,
pubmed-meshheading:1815636-Purine Nucleotides,
pubmed-meshheading:1815636-Pyrimidine Nucleotides,
pubmed-meshheading:1815636-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1815636-Software,
pubmed-meshheading:1815636-Thermodynamics
|
pubmed:year |
1991
|
pubmed:articleTitle |
Theoretical study of ethidium intercalation in triple-stranded DNA and at triplex-duplex junctions.
|
pubmed:affiliation |
Laboratoire de Biophysique, INSERM U201, CNRS UA481, Paris, France.
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pubmed:publicationType |
Journal Article
|