Polyelectrolyte behavior and kinetics of aminoacyl-tRNA on the ribosome

A. Spasic, S. Sitha, M. Korchak, S. Chu, U. Shanty

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)4161-4163
Number of pages3
JournalJournal of Physical Chemistry B
Issue number14
Publication statusPublished - 10 Apr 2008
Externally publishedYes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry


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