| pubmed-article:15888729 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15888729 | lifeskim:mentions | umls-concept:C0011524 | lld:lifeskim |
| pubmed-article:15888729 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:15888729 | lifeskim:mentions | umls-concept:C1149286 | lld:lifeskim |
| pubmed-article:15888729 | lifeskim:mentions | umls-concept:C0449774 | lld:lifeskim |
| pubmed-article:15888729 | lifeskim:mentions | umls-concept:C0205214 | lld:lifeskim |
| pubmed-article:15888729 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:15888729 | pubmed:dateCreated | 2005-5-12 | lld:pubmed |
| pubmed-article:15888729 | pubmed:abstractText | Restriction enzymes are among the best studied examples of DNA binding proteins. In order to find general patterns in DNA recognition sites, which may reflect important properties of protein-DNA interaction, we analyse the binding sites of all known type II restriction endonucleases. We find a significantly enhanced GC content and discuss three explanations for this phenomenon. Moreover, we study patterns of nucleotide order in recognition sites. Our analysis reveals a striking accumulation of adjacent purines (R) or pyrimidines (Y). We discuss three possible reasons: RR/YY dinucleotides are characterized by (i) stronger H-bond donor and acceptor clusters, (ii) specific geometrical properties and (iii) a low stacking energy. These features make RR/YY steps particularly accessible for specific protein-DNA interactions. Finally, we show that the recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes. | lld:pubmed |
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| pubmed-article:15888729 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15888729 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15888729 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15888729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15888729 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15888729 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:15888729 | pubmed:author | pubmed-author:BeyerAndreasA | lld:pubmed |
| pubmed-article:15888729 | pubmed:author | pubmed-author:WilhelmThomas... | lld:pubmed |
| pubmed-article:15888729 | pubmed:author | pubmed-author:HollunderJens... | lld:pubmed |
| pubmed-article:15888729 | pubmed:author | pubmed-author:NikolajewaSve... | lld:pubmed |
| pubmed-article:15888729 | pubmed:author | pubmed-author:FriedelMaikM | lld:pubmed |
| pubmed-article:15888729 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15888729 | pubmed:volume | 33 | lld:pubmed |
| pubmed-article:15888729 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15888729 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15888729 | pubmed:pagination | 2726-33 | lld:pubmed |
| pubmed-article:15888729 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:15888729 | pubmed:meshHeading | pubmed-meshheading:15888729... | lld:pubmed |
| pubmed-article:15888729 | pubmed:meshHeading | pubmed-meshheading:15888729... | lld:pubmed |
| pubmed-article:15888729 | pubmed:meshHeading | pubmed-meshheading:15888729... | lld:pubmed |
| pubmed-article:15888729 | pubmed:meshHeading | pubmed-meshheading:15888729... | lld:pubmed |
| pubmed-article:15888729 | pubmed:meshHeading | pubmed-meshheading:15888729... | lld:pubmed |
| pubmed-article:15888729 | pubmed:meshHeading | pubmed-meshheading:15888729... | lld:pubmed |
