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  The three conformations of the anticodon loop of yeast tRNA(Phe).

Striker, G., Labuda, D., & Vega-Martin, M. (1989). The three conformations of the anticodon loop of yeast tRNA(Phe). Journal of Biomolecular Structure and Dynamics, 7(2), 235-255. doi:10.1080/07391102.1989.10507768.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-2B4D-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-2B50-9
Genre: Journal Article

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Striker, G.1, Author              
Labuda, D., Author
Vega-Martin, M., Author
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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 Abstract: The complex conformational states of the anticodon loop of yeast tRNAPhe which we had previously studied with relaxation experiments by monitoring fluorescence of the naturally occuring Wye base, are analyzed using time and polarization resolved fluorescence measurements at varying counterion concentrations. Synchrotron radiation served as excitation for these experiments, which were analyzed using modulating functions and global methods. Three conformations of the anticodon loop are detected, all three occuring in a wide range of counterion concentrations with and without Mg2+, each being identified by its typical lifetime. The fluorescence changes brought about by varying the ion concentrations, previously monitored by steady state fluorimetry and relaxation methods, are changes in the population of these three conformational states, in the sense of an allosteric model, where the effectors are the three ions Mg2+, Na+ and H+. The population of the highly fluorescent M conformer (8ns), most affine to magnesium, is thus enhanced by that ligand, while the total fluorescence decreases as lower pH favors the H+-affine H conformer (0.6ns). Na+-binding of the N conformer (4ns) is responsible for complex fluorescence changes. By iterative simulation of this allosteric model the equilibrium and binding constants are determined. In turn, using these constants to simulate equilibrium fluorescence titrations reproduces the published results.

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Language(s): eng - English
 Dates: 2012-05-211989-10
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1080/07391102.1989.10507768
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Title: Journal of Biomolecular Structure and Dynamics
Source Genre: Journal
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Pages: - Volume / Issue: 7 (2) Sequence Number: - Start / End Page: 235 - 255 Identifier: -