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How fast a post-translational nascent protein escapes from the ribosomal exittunnel is relevant to its folding and protection against aggregation. Here, byusing Langevin molecular dynamics, we show that non-local native interactionshelp decreasing the escape time, and foldable proteins generally escape muchfaster than same-length self-repulsive homopolymers at low temperatures. Theescape process, however, is slowed down by the local interactions thatstabilize the {\alpha}-helices. The escape time is found to increase with boththe tunnel length and the concentration of macromolecular crowders outside thetunnel. We show that a simple diffusion model described by the Smoluchowskiequation with an effective linear potential can be used to map out the escapetime distribution for various tunnel lengths and various crowderconcentrations. The consistency between the simulation data and the diffusionmodel however is found only for the tunnel length smaller than a cross-overlength of 90 {\AA} to 110 {\AA}, above which the escape time increases muchfaster with the tunnel length. It is suggested that the length of ribosomalexit tunnel has been selected by evolution to facilitate both the efficientfolding and efficient escape of single domain proteins. We show thatmacromolecular crowders lead to an increase of the escape time, and attractivecrowders are unfavorable for the folding of nascent polypeptide.

Protein escape at the ribosomal exit tunnel: Effects of native interactions, tunnel length and macromolecular crowding