Ribosomes are assembled from both protein (r-protein) and RNA (rRNA) by a process that has been studied extensively in the past 50 years. However, while experimental evidence suggests that prokaryotic r-proteins undergo computational changes during assembly, to date, no studies have been done to explore the computational changes that occur.   In this project, the details of the dynamics of S7 (a primary r-protein), S6, and S18 from the E. coli 30S subunit and S7 from the T. thermophilus 30S subunit were studied using molecular dynamic (MD) simulations.  MD results reveal that S7 retains the same conformation in solution as in the assembled unit and the residues contacting the rRNA are generally more mobile in comparison with the other non-contacting residues, whereas S6 and S18 do not share this trend of more mobile contact residues.

Quantifying conformational changes of ribosomal proteins S7, S6, and S18

243rd National Meeting (2012)

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