ABSTRACT
The torque acting on cognate (three base pairs that are matched) "ternary complex" consisting of elongation factor-Tu, guanosine-5'-triphosphate GTP, and aminoacyl-transfer RNA due to induced wrapping of the 30S subunit of the ribosome and the speed with which the ternary complex samples the space allowed by diffusion is determined. Under appropriate conditions, mode coupling speeds up the barrier crossing rate for cognate relative to near-cognate ternary complexes. We determine the flexibility of the ternary complex relative to transfer RNA (tRNA) by a coarse-grained model. We predict the magnesium binding sites in the ternary complex at low magnesium concentration and unravel the nature of the interaction energy of magnesium with site-specific tRNAPhe bases.
