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  Dynamics of the RNA hairpin GNRA tetraloop

Menger, M., Eckstein, F., & Porschke, D. (2000). Dynamics of the RNA hairpin GNRA tetraloop. Biochemistry, 39: 10.1021/bi992297n, pp. 4500-4507.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F8F3-F Version Permalink: http://hdl.handle.net/21.11116/0000-0002-0329-D
Genre: Journal Article

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Menger, M.1, Author              
Eckstein, F., Author
Porschke, D.2, Author              
Affiliations:
1Abteilung Biochemische Kinetik, MPI for biophysical chemistry, Max Planck Society, ou_578616              
2Research Group of Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578610              

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 Abstract: The dynamics of RNA hairpin tetraloops of the GNRA type [sequence G- any ribonucleotide (N)-purine (R)-A] was analyzed by fluorescence spectroscopy and by fluorescence-detected temperature jump relaxation, using RNA oligomers with 2-aminopurine (2AP) substituted in two different positions of the loop sequence, Gp2APpApA (HP1) and GpAp2APpA (HP2), as indicator. The fluorescence of HP1 is much higher than that of HP2, indicating a lower degree of 2AP-stacking in HP1. Addition of Mg2+ or Ca2+ ions leads to an increase of fluorescence in HP1, whereas a decrease of fluorescence is observed in HP2. In both cases at least two ion-binding equilibria are required to fit titration data. T-jump experiments using fluorescence detection show a relaxation process with a time constant of 22 µs for HP1, whereas two relaxation processes with time constants 5 and 41 µs, are found for HP2. These results clearly demonstrate the existence of more than the single conformation state detected by NMR analysis. The T-jump amplitudes decrease with increasing bivalent ion concentration, indicating that one of the states is favored in the presence of bivalent ions. The loop relaxation processes are slower than standard stacking processes, probably because of activation barriers imposed by a restricted mobility of loop residues, and are assigned to a stacking rearrangement, probably between the 5' and the 3'-side. A similar process has been observed previously for the anticodon loop of tRNAPhe. The rate constants of the transition are in the range of 104 s-1 in the case of HP1. The data demonstrate the existence of structures that are not resolved by standard NMR because of fast exchange and are not found by X-ray analysis because of restrictions by crystal packing.

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Language(s): eng - English
 Dates: 2005-08-172000
 Publication Status: Published in print
 Pages: -
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 Rev. Method: -
 Identifiers: eDoc: 231148
Other: 23136
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Title: Biochemistry
Source Genre: Journal
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Pages: - Volume / Issue: 39 Sequence Number: 10.1021/bi992297n Start / End Page: 4500 - 4507 Identifier: -