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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2002-5-22
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pubmed:abstractText |
The amino group of adenine plays a key role in maintaining DNA triple helical structures, being the only functional group in DNA that is involved in both Watson-Crick and Hoogsteen hydrogen bonds. In the present work we have probed the internal dynamics of the adenine amino group in the intramolecular YRY triple helix formed by the 31-mer DNA oligonucleotide d(AGAGAGAACCCCTTCTCTCTTTTTCTCTCTT). The DNA triple helix was specifically labeled with (15)N at the amino group of the adenine in the fifth position. The rotation rate of the labeled amino group was measured as a function of temperature using (1)H-(15)N heteronuclear NMR spectroscopy. The results indicate that, in the DNA triple helix, the rotation of the adenine amino group is greatly slowed relative to that in a DNA double helix. The temperature dependence of the rotation rate suggests a large entropic contribution to this effect, which may originate from different hydration patterns of the adenine amino group in the two structures.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-10233082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-11551203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-1318385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-1731320,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-1731886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-1738161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-1896473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-1946419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-3293213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-7522550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-7574496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-7663120,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-8081755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-8599672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-9477975,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12023242-9478127
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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 |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
82
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3181-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12023242-Adenine,
pubmed-meshheading:12023242-Base Sequence,
pubmed-meshheading:12023242-Biophysical Phenomena,
pubmed-meshheading:12023242-Biophysics,
pubmed-meshheading:12023242-DNA,
pubmed-meshheading:12023242-Hydrogen Bonding,
pubmed-meshheading:12023242-Nitrogen Isotopes,
pubmed-meshheading:12023242-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:12023242-Nucleic Acid Conformation,
pubmed-meshheading:12023242-Oligodeoxyribonucleotides,
pubmed-meshheading:12023242-Protons
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pubmed:year |
2002
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pubmed:articleTitle |
Internal dynamics in a DNA triple helix probed by (1)H-(15)N-NMR spectroscopy.
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pubmed:affiliation |
Department of Molecular Biology and Biochemistry, Molecular Biophysics Program, Wesleyan University, Middletown, Connecticut 06459, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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