A. Bonincontro et al., A STUDY OF THE DIELECTRIC-PROPERTIES OF ESCHERICHIA-COLI RIBOSOMAL-RNA AND PROTEINS IN SOLUTION, Biophysical chemistry, 67(1-3), 1997, pp. 43-50
The permittivity of ribosomal proteins and ribosomal RNA (rRNA) in sol
ution was measured in the range 100 kHz to 1 GHz at four different tem
peratures (5, 15, 25 and 35 degrees C). The experimental dielectric re
laxation was analysed by the Cole-Cole equation and, from the best-fit
parameters, the average values of the dipole moment and molecular rad
ius of the proteins were obtained. The activation enthalpy was calcula
ted from an Arrhenius plot of the relaxation time. The energy involved
in the dielectric polarization of free proteins has a magnitude of ab
out one hydrogen bond. The data on RNA were analysed according to the
Mandel model. This analysis allowed the calculation of the ''subunit b
'' as defined by Mandel. This parameter is dependent on the temperatur
e and therefore the relaxation time does not follow the Arrhenius law.
Our data thus show that, in solution, the rRNA structure is thermally
rather unstable and highly flexible. (C) 1997 Elsevier Science B.V.