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The Dynamics of Unfolded Versus Folded tRNA: The Role of Electrostatic Interactions



Joon Ho Roh, Madhu Sudan Tyagi, Robert M. Briber, Sarah A. Woodson, Alexei P. Sokolov


We have used quasielastic neutron scattering spectroscopy to study the dynamics of unfolded tRNA under low ionic strength and tRNA folded through the addition of Mg2+ in order to examine the role of electrostatic interactions in the dynamics of biological polyelectrolytes. Analyses of the atomic mean-squared displacement, relaxation time, molecular persistency, and mobile fraction showed that unfolded tRNA is dynamically more rigid due to intrinsic electrostatic repulsion than Mg2+ folded tRNA. This same result is found for a sulfonated polystyrene, a synthetic polyelectrolyte, where the system is dynamically more rigid in the unscreened state compared to the counterion screened state. These results are contrary the relationship between structural compactness and internal dynamics for proteins where the folded state is observed to be more rigid than denatured state. This implies that the dynamics of biological polyelectrolytes are strongly influenced by electrostatic environments rather than solely controlled by the dynamics of the local water.
Journal of American Chemical Society


Dynamics, t-RNA, protein, quasi-elastic neutron scattering


Roh, J. , Tyagi, M. , Briber, R. , Woodson, S. and Sokolov, A. (2011), The Dynamics of Unfolded Versus Folded tRNA: The Role of Electrostatic Interactions, Journal of American Chemical Society, [online], (Accessed April 19, 2024)
Created September 20, 2011, Updated October 12, 2021