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. 2013 May 31;110(25):10195–10200. doi: 10.1073/pnas.1307869110

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Fig. 5. — The free-energy surface for the chain motion in the ribosome/TR system in the effective x₁, z_m space. The figure shows that the least energy path must involve a diagonal motion along the z_m = –x₁ path so that the chemical barrier will not be added to the TR barrier. The figure presents the least energy path for L = 24 (A) and L = 30 (B), showing that the stall barrier is drastically reduced for L = 30, where the chain can now pass the TR barrier overcoming the effect of stall. The schematic figures on the side panels show the configurations of the chain. The overall length of the chain folded in between the ribosome and TR is denoted by 2z_m. The barriers used for the regular chemical, TR insertion, and the stall chemical processes are 15, 18, and 22 kcal/mol, respectively. The x₁ scale reflects an extension of the H segment.

Inline graphic — The free-energy surface for the chain motion in the ribosome/TR system in the effective x₁, z_m space. The figure shows that the least energy path must involve a diagonal motion along the z_m = –x₁ path so that the chemical barrier will not be added to the TR barrier. The figure presents the least energy path for L = 24 (A) and L = 30 (B), showing that the stall barrier is drastically reduced for L = 30, where the chain can now pass the TR barrier overcoming the effect of stall. The schematic figures on the side panels show the configurations of the chain. The overall length of the chain folded in between the ribosome and TR is denoted by 2z_m. The barriers used for the regular chemical, TR insertion, and the stall chemical processes are 15, 18, and 22 kcal/mol, respectively. The x₁ scale reflects an extension of the H segment.