| pubmed-article:10471730 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10471730 | lifeskim:mentions | umls-concept:C0035711 | lld:lifeskim |
| pubmed-article:10471730 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:10471730 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
| pubmed-article:10471730 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:10471730 | lifeskim:mentions | umls-concept:C2003939 | lld:lifeskim |
| pubmed-article:10471730 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:10471730 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:10471730 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
| pubmed-article:10471730 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:10471730 | pubmed:dateCreated | 1999-11-4 | lld:pubmed |
| pubmed-article:10471730 | pubmed:abstractText | Sequence-specific interactions between aminoacyl-tRNA synthetases and their cognate tRNAs ensure both accurate RNA recognition and the efficient catalysis of aminoacylation. The effects of tRNA(Trp)variants on the aminoacylation reaction catalyzed by wild-type Escherichia coli tryptophanyl-tRNA synthe-tase (TrpRS) have now been investigated by stopped-flow fluorimetry, which allowed a pre-steady-state analysis to be undertaken. This showed that tRNA(Trp)identity has some effect on the ability of tRNA to bind the reaction intermediate TrpRS-tryptophanyl-adenylate, but predominantly affects the rate at which trypto-phan is transferred from TrpRS-tryptophanyl adenylate to tRNA. Use of the binding ( K (tRNA)) and rate constants ( k (4)) to determine the energetic levels of the various species in the aminoacylation reaction showed a difference of approximately 2 kcal mol(-1)in the barrier to transition state formation compared to wild-type for both tRNA(Trp)A-->C73 and. These results directly show that tRNA identity contributes to the degree of complementarity to the transition state for tRNA charging in the active site of an aminoacyl-tRNA synthetase:aminoacyl-adenylate:tRNA complex. | lld:pubmed |
| pubmed-article:10471730 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10471730 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10471730 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10471730 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10471730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10471730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10471730 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10471730 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10471730 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:10471730 | pubmed:author | pubmed-author:SöllDD | lld:pubmed |
| pubmed-article:10471730 | pubmed:author | pubmed-author:HiteA FAF | lld:pubmed |
| pubmed-article:10471730 | pubmed:author | pubmed-author:SeverSS | lld:pubmed |
| pubmed-article:10471730 | pubmed:author | pubmed-author:Praetorius-Ib... | lld:pubmed |
| pubmed-article:10471730 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:10471730 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10471730 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:10471730 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10471730 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10471730 | pubmed:pagination | 3631-7 | lld:pubmed |
| pubmed-article:10471730 | pubmed:dateRevised | 2008-11-20 | lld:pubmed |
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| pubmed-article:10471730 | pubmed:meshHeading | pubmed-meshheading:10471730... | lld:pubmed |
| pubmed-article:10471730 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10471730 | pubmed:articleTitle | Transfer RNA identity contributes to transition state stabilization during aminoacyl-tRNA synthesis. | lld:pubmed |
| pubmed-article:10471730 | pubmed:affiliation | Department of Molecular Biophysics and Biochemistry Yale University, New Haven, CT 06520-8114, USA. mibba@imbg.ku.dk | lld:pubmed |
| pubmed-article:10471730 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10471730 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:10471730 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:947894 | entrezgene:pubmed | pubmed-article:10471730 | lld:entrezgene |
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