The dynamics of tRNAPhe from brewer's yeast in solution was studied over a broad concentration and temperature range by polarized and depolarized dynamic light scattering. It is shown that measurements of the depolarized Rayleigh spectrum with a high-resolution confocal Fabry-Perot interferometer pr
Internal dynamics of tRNAPhe studied by depolarized dynamic light scattering
✍ Scribed by A. Patkowski; W. Eimer; Th. Dorfmüller
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1990
- Tongue
- English
- Weight
- 739 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
The collective internal dynamics of transfer RNAPhe from brewer's yeast in solution was studied by depolarized dynamic light scattering (DDLS) . Within the melting region of tRNA the depolarized spectra consist of two Lorentzian, where the narrow (slow) component describes the overall rotation of the macromolecule. The broad component is attributed to the collective reorientation of the bases within the biopolymer. At high temperature only this relaxation process is observed in the spectrum. The viscosity dependence of the collective internal relaxation process is described by the Stokes-Einstein-Debye equation for rotational diffusion. Estimates of the internal orientational pair correlation factor from the integral depolarized intensities of tRNAPhe solutions indicates that the observed dynamics correspond to the collective reorientation of approximately 5 bases. A comparison of the results presented with DDLS studies on the aggregation of the mononucleotide guanosine-5'-monophosphate confirms this result. For a further characterization of the relaxation process we studied the effect of hydrostatic pressure (1-1000 bar) on the depolarized spectra of tRNA. While other spectroscopic methods like nmr, fluorescence polarization anisotropy decay, or ESR give information about the very local motion of a single base within the DNA or RNA, this study shows that by DDLS one can characterize collective internal motions of macromolecules.
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