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- W2952502424 abstract "Abstract The accurate expression of proteins requires the ribosome to efficiently undergo elaborate conformational rearrangements. The most dramatic of these motions is subunit rotation, which is necessary for tRNA molecules to transition between ribosomal binding sites. While rigid-body descriptions provide a qualitative picture of the process, obtaining quantitative mechanistic insights requires one to account for the relationship between molecular flexibility and collective dynamics. Using simulated rotation events, we assess the quality of experimentally-accessible measures for describing the collective displacement of the ~ 4000-residue small subunit. For this, we ask whether each coordinate is able to identify the underlying free-energy barrier and transition state ensemble (TSE). We find that intuitive structurally-motivated coordinates (e.g. rotation angle, inter-protein distances) can distinguish between the endpoints, though they are poor indicators of barrier-crossing events, and they underestimate the free-energy barrier. In contrast, coordinates based on inter-subunit bridges can identify the TSE. We additionally verify that the committor probability for the putative TSE configurations is 0.5, a hallmark feature of any transition state. In terms of structural properties, these calculations implicate a transition state in which flexibility allows for asynchronous rearrangements of the bridges as the ribosome adopts a partially-rotated orientation. These calculations provide a theoretical foundation, upon which experimental techniques may precisely quantify the energy landscape of the ribosome." @default.
- W2952502424 created "2019-06-27" @default.
- W2952502424 creator A5009964626 @default.
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- W2952502424 date "2019-01-08" @default.
- W2952502424 modified "2023-09-25" @default.
- W2952502424 title "Dissecting the energetics of subunit rotation in the ribosome" @default.
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- W2952502424 doi "https://doi.org/10.1101/514448" @default.
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