Molekulare Erkennung eines Minimalmodells der aminoacylierten tRNA durch den Elongationsfaktor Tu der bakteriellen Proteinbiosynthese
- 14 November 1997
- journal article
- zuschrift
- Published by Wiley in Angewandte Chemie
- Vol. 109 (22) , 2592-2596
- https://doi.org/10.1002/ange.19971092224
Abstract
Spezifisch gebunden wird 1an den Elongationsfaktor Tu der bakteriellen Proteinbiosynthese. Aus detaillierten NMR‐Untersuchungen können die Struktur und die Bindungscharakteristika bei der molekularen Erkennung von1, das als Mimeticum der korrekt aminoacylierten tRNA fungiert, abgeleitet werden. magnified imageKeywords
This publication has 20 references indexed in Scilit:
- The Structure of 3'-O-Anthraniloyladenosine, an Analogue of the 3-End of Aminoacyl-tRNANucleic Acids Research, 1997
- Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP AnalogScience, 1995
- Minimalist Aminoacylated RNAs as Efficient Substrates for Elongation Factor TuBiochemistry, 1994
- tRNA fluorescent labeling at 3′ end inducing an aminoacyl‐tRNA‐like behaviorEuropean Journal of Biochemistry, 1993
- Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMRBiochemistry, 1992
- Aminoacyl-tRNA Exclusively in the 3′-Isomeric Form Is Bound to Polypeptide Chain Elongation Factor Tu1The Journal of Biochemistry, 1985
- Rate of Transacylation between 2′ and 3′-O-L-PhenyIalanyIadenosineThe Journal of Biochemistry, 1981
- TIME-DEPENDENT PHENOMENA AND PROBLEMS OF AVERAGINGPublished by Elsevier ,1981
- Interaction of Escherichia coli EF‐Tu · GTP and EF‐Tu · GDP with Analogues of the 3′ Terminus of Aminoacyl‐tRNAEuropean Journal of Biochemistry, 1980
- The binding site for the 3′‐terminus of aminoacyl‐tRNA in the molecule of elongation factor Tu from Escherichia coliFEBS Letters, 1979