Abstract
Dynamics of tRNA was studied using neutron scattering spectroscopy. Despite vast differences in the architecture and backbone structure of proteins and RNA, hydrated tRNA undergoes the dynamic transition at the same temperature as hydrated lysozyme. The similarity of the dynamic transition in RNA and proteins supports the idea that it is solvent induced. Because tRNA essentially has no methyl groups, the results also suggest that methyl groups are not the main contributor of the dynamic transition in biological macromolecules. However, they may explain strong differences in the dynamics of tRNA and lysozyme observed at low temperatures.
Original language | English |
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Pages (from-to) | 32-33 |
Number of pages | 2 |
Journal | Journal of the American Chemical Society |
Volume | 128 |
Issue number | 1 |
DOIs | |
State | Published - Jan 11 2006 |
Externally published | Yes |