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Significance Mechanochemistry, the influence of molecular-scale mechanical forces on chemical processes, can occur on actively translating ribosomes through the force-generating actions of motor proteins and the cotranslational folding of domains. Such forces are transmitted to the ribosome’s catalytic core and alter rates of protein synthesis, representing a form of mechanical allosteric communication. These changes in translation–elongation kinetics are biologically important because they can influence protein structure, function, and localization within a cell. Many fundamental questions are unresolved concerning the properties of protein domains that determine mechanical force generation; the effect of translation speed on this force; and exactly how, at the molecular level, force is generated. In this study we answer these questions using molecular simulations and statistical mechanical modeling.

Domain topology, stability, and translation speed determine mechanical force generation on the ribosome