| pubmed-article:9054966 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9054966 | lifeskim:mentions | umls-concept:C0012634 | lld:lifeskim |
| pubmed-article:9054966 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:9054966 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:9054966 | lifeskim:mentions | umls-concept:C0030943 | lld:lifeskim |
| pubmed-article:9054966 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:9054966 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:9054966 | lifeskim:mentions | umls-concept:C0525015 | lld:lifeskim |
| pubmed-article:9054966 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:9054966 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:9054966 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9054966 | pubmed:dateCreated | 1997-4-3 | lld:pubmed |
| pubmed-article:9054966 | pubmed:abstractText | Initiation factor IF3 from Escherichia coli plays a critical role in the selection of the correct initiation codon. This protein is composed of two domains, connected by a lysin-rich hydrophilic linker. The conformation of native IF3 was investigated by heteronuclear NMR spectroscopy. The two domains are independent and show little or no interaction. Heteronuclear relaxation studies of a sample selectively labelled on lysine residues demonstrates that the inter-domain linker is highly flexible, exhibiting increased 15N T2 values and negative 1H[15N] nuclear Overhause effects over a length of at least eight residues. Analysis of the rotational correlation times further shows that the motions of the two domains are most likely uncorrelated. The inter-domain linker thus displays almost totally unrestricted motions. Accordingly, the amide protons in the central region are shown to be in fast exchange with water. Such a high degree of flexibility of the inter-domain linker might be required for IF3 domains to interact with distant regions of the ribosome. | lld:pubmed |
| pubmed-article:9054966 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9054966 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9054966 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9054966 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9054966 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9054966 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9054966 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9054966 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9054966 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9054966 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9054966 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:9054966 | pubmed:author | pubmed-author:BlanquetSS | lld:pubmed |
| pubmed-article:9054966 | pubmed:author | pubmed-author:MoreauMM | lld:pubmed |
| pubmed-article:9054966 | pubmed:author | pubmed-author:GarciaCC | lld:pubmed |
| pubmed-article:9054966 | pubmed:author | pubmed-author:LallemandJ... | lld:pubmed |
| pubmed-article:9054966 | pubmed:author | pubmed-author:DardelFF | lld:pubmed |
| pubmed-article:9054966 | pubmed:author | pubmed-author:AlbaretCC | lld:pubmed |
| pubmed-article:9054966 | pubmed:author | pubmed-author:FortierP LPL | lld:pubmed |
| pubmed-article:9054966 | pubmed:author | pubmed-author:de CockEE | lld:pubmed |
| pubmed-article:9054966 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9054966 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:9054966 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:9054966 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9054966 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9054966 | pubmed:pagination | 15-22 | lld:pubmed |
| pubmed-article:9054966 | pubmed:dateRevised | 2002-11-1 | lld:pubmed |
| pubmed-article:9054966 | pubmed:meshHeading | pubmed-meshheading:9054966-... | lld:pubmed |
| pubmed-article:9054966 | pubmed:meshHeading | pubmed-meshheading:9054966-... | lld:pubmed |
| pubmed-article:9054966 | pubmed:meshHeading | pubmed-meshheading:9054966-... | lld:pubmed |
| pubmed-article:9054966 | pubmed:meshHeading | pubmed-meshheading:9054966-... | lld:pubmed |
| pubmed-article:9054966 | pubmed:meshHeading | pubmed-meshheading:9054966-... | lld:pubmed |
| pubmed-article:9054966 | pubmed:meshHeading | pubmed-meshheading:9054966-... | lld:pubmed |
| pubmed-article:9054966 | pubmed:meshHeading | pubmed-meshheading:9054966-... | lld:pubmed |
| pubmed-article:9054966 | pubmed:meshHeading | pubmed-meshheading:9054966-... | lld:pubmed |
| pubmed-article:9054966 | pubmed:meshHeading | pubmed-meshheading:9054966-... | lld:pubmed |
| pubmed-article:9054966 | pubmed:meshHeading | pubmed-meshheading:9054966-... | lld:pubmed |
| pubmed-article:9054966 | pubmed:meshHeading | pubmed-meshheading:9054966-... | lld:pubmed |
| pubmed-article:9054966 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9054966 | pubmed:articleTitle | Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution. | lld:pubmed |
| pubmed-article:9054966 | pubmed:affiliation | Laboratoire de Synthèse Organique, URA 1308 du CNRS Ecole Polytechnique, Palaiseau, France. | lld:pubmed |
| pubmed-article:9054966 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:946225 | entrezgene:pubmed | pubmed-article:9054966 | lld:entrezgene |
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