Hydrophobic and electrostatic interactions modulate protein escape at the ribosomal exit tunnel.

ABSTRACT: After translation, nascent proteins must escape the ribosomal exit tunnel to attain complete folding to their native states. This escape process also frees up the ribosome tunnel for a new translation job. In this study, we investigate the impacts of energetic interactions between the ribosomal exit tunnel and nascent proteins on the protein escape process by molecular dynamics simulations using partially coarse-grained models that incorporate hydrophobic and electrostatic interactions of the ribosome tunnel of Haloarcula marismortui with nascent proteins. We find that, in general, attractive interactions slow down the protein escape process, whereas repulsive interactions speed it up. For the small globular proteins considered, the median escape time correlates with both the number of hyd

SUBMITTER: Bui PT 

PROVIDER: S-EPMC8595739 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature