pubmed-article:1447218 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1447218 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
pubmed-article:1447218 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:1447218 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:1447218 | lifeskim:mentions | umls-concept:C0205099 | lld:lifeskim |
pubmed-article:1447218 | lifeskim:mentions | umls-concept:C0599533 | lld:lifeskim |
pubmed-article:1447218 | pubmed:issue | 34 | lld:pubmed |
pubmed-article:1447218 | pubmed:dateCreated | 1992-12-30 | lld:pubmed |
pubmed-article:1447218 | pubmed:abstractText | We have probed the contacts between EcoRI endonuclease and the central phosphate of its recognition site GAApTTC, using synthetic oligonucleotides containing single stereospecific Rp- or Sp-phosphorothioates (Ps). These substitutions produce subtle stereospecific effects on EcoRI endonuclease binding and cleavage. An Sp-Ps substitution in one strand of the DNA duplex improves binding free energy by -1.5 kcal/mol, whereas the Rp-Ps substitution has an unfavorable effect (+0.3 kcal/mol) on binding free energy. These effects derive principally from changes in the first order rate constants for dissociation of the enzyme-DNA complexes. The first order rate constants for strand scission are also affected, in that a strand containing Sp-Ps substitution is cleaved 2 to 3 times more rapidly than a strand containing a normal prochiral phosphate, whereas a strand containing Rp-Ps substitution is cleaved about 3 times slower than normal. As a result, single-strand substitutions produce pronounced asymmetry in the rates of cleavage of the two DNA strands, and this effect is exaggerated in an Rp,Sp-heteroduplex. Ethylation-interference footprinting indicates that none of the Ps substitutions cause any major change in contacts between endonuclease and DNA phosphates. When an Sp-Ps localizes P = O in the DNA major groove, a hydrogen-bonding interaction with the backbone amide-NH of Gly116 of the endonuclease is improved relative to that with a prochiral phosphate having intermediate P-O bond order and delocalized charge. | lld:pubmed |
pubmed-article:1447218 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1447218 | pubmed:language | eng | lld:pubmed |
pubmed-article:1447218 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1447218 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1447218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1447218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1447218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1447218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1447218 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1447218 | pubmed:month | Dec | lld:pubmed |
pubmed-article:1447218 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:1447218 | pubmed:author | pubmed-author:StecW JWJ | lld:pubmed |
pubmed-article:1447218 | pubmed:author | pubmed-author:Koziolkiewicz... | lld:pubmed |
pubmed-article:1447218 | pubmed:author | pubmed-author:Jen-JacobsonL... | lld:pubmed |
pubmed-article:1447218 | pubmed:author | pubmed-author:KurpiewskiM... | lld:pubmed |
pubmed-article:1447218 | pubmed:author | pubmed-author:GrajkowskiAA | lld:pubmed |
pubmed-article:1447218 | pubmed:author | pubmed-author:LesserD RDR | lld:pubmed |
pubmed-article:1447218 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1447218 | pubmed:day | 5 | lld:pubmed |
pubmed-article:1447218 | pubmed:volume | 267 | lld:pubmed |
pubmed-article:1447218 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1447218 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1447218 | pubmed:pagination | 24810-8 | lld:pubmed |
pubmed-article:1447218 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:1447218 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1447218 | pubmed:articleTitle | Stereoselective interaction with chiral phosphorothioates at the central DNA kink of the EcoRI endonuclease-GAATTC complex. | lld:pubmed |
pubmed-article:1447218 | pubmed:affiliation | Department of Biological Sciences, University of Pittsburgh, Pennsylvania 15260. | lld:pubmed |
pubmed-article:1447218 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1447218 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:1447218 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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