The Physical Factors Governing Tensile Force Generation by Co-translational Protein Folding

Abstract

Tensile forces generated from co-translational protein folding can affect the translation elongation rate, which will in turn modify the protein's ability to fold and function properly. Here, we use computational methods to determine the magnitude and scaling of the tensile forces generated by the co-translational folding of several protein domains. We also use these domains to determine how the magnitude of the tensile force depends on physical factors, especially domain stability and topology. These results show that co-translational folding can exert a force which can influence the translation elongation rate, including rescuing a stalled sequence. This force is biologically significant because it can change the orientation of the PTC, which can change translation elongation rates, which affects co-translational folding and other downstream processes.