| pubmed-article:11433029 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11433029 | lifeskim:mentions | umls-concept:C0012935 | lld:lifeskim |
| pubmed-article:11433029 | lifeskim:mentions | umls-concept:C0600500 | lld:lifeskim |
| pubmed-article:11433029 | lifeskim:mentions | umls-concept:C0920283 | lld:lifeskim |
| pubmed-article:11433029 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:11433029 | lifeskim:mentions | umls-concept:C0242485 | lld:lifeskim |
| pubmed-article:11433029 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
| pubmed-article:11433029 | lifeskim:mentions | umls-concept:C1819424 | lld:lifeskim |
| pubmed-article:11433029 | lifeskim:mentions | umls-concept:C0549193 | lld:lifeskim |
| pubmed-article:11433029 | lifeskim:mentions | umls-concept:C1524063 | lld:lifeskim |
| pubmed-article:11433029 | lifeskim:mentions | umls-concept:C0173731 | lld:lifeskim |
| pubmed-article:11433029 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:11433029 | pubmed:dateCreated | 2001-7-2 | lld:pubmed |
| pubmed-article:11433029 | pubmed:abstractText | Measurement of steady-state rates of unwinding of double-stranded oligonucleotides by helicases is hampered due to rapid reannealing of the single-stranded DNA products. Including an oligonucleotide in the reaction mixture which can hybridize with one of the single strands can prevent reannealing. However, helicases bind to single-stranded DNA, therefore the additional oligonucleotide can sequester the enzyme, leading to slower observed rates for unwinding. To circumvent this problem, the oligonucleotide that serves as a trap was replaced with a strand of peptide nucleic acid (PNA). Fluorescence polarization was used to determine that a 15mer PNA strand does not bind to the bacteriophage T4 Dda helicase. Steady-state kinetic parameters of unwinding catalyzed by Dda were determined by using PNA as a trapping strand. The substrate consisted of a partial duplex with 15 nt of single-stranded DNA and 15 bp. In the presence of 250 nM substrate and 1 nM Dda, the rate of unwinding in the presence of the DNA trapping strand was 0.30 nM s(-1) whereas the rate was 1.34 nM s(-1) in the presence of the PNA trapping strand. PNA prevents reannealing of single-stranded DNA products, but does not sequester the helicase. This assay will prove useful in defining the complete kinetic mechanism for unwinding of oligonucleotide substrates by this helicase. | lld:pubmed |
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| pubmed-article:11433029 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11433029 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11433029 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11433029 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11433029 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11433029 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:11433029 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:11433029 | pubmed:author | pubmed-author:RaneyK DKD | lld:pubmed |
| pubmed-article:11433029 | pubmed:author | pubmed-author:NanduriBB | lld:pubmed |
| pubmed-article:11433029 | pubmed:author | pubmed-author:TackettA JAJ | lld:pubmed |
| pubmed-article:11433029 | pubmed:author | pubmed-author:EoffR LRL | lld:pubmed |
| pubmed-article:11433029 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:11433029 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11433029 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:11433029 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11433029 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11433029 | pubmed:pagination | 2829-35 | lld:pubmed |
| pubmed-article:11433029 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11433029 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11433029 | pubmed:articleTitle | Measurement of steady-state kinetic parameters for DNA unwinding by the bacteriophage T4 Dda helicase: use of peptide nucleic acids to trap single-stranded DNA products of helicase reactions. | lld:pubmed |
| pubmed-article:11433029 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, 4301 West Markham, Little Rock, AR 72205, USA. | lld:pubmed |
| pubmed-article:11433029 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11433029 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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