Annealing synchronizes the 70 S ribosome into a minimum-energy conformation

Abstract

Significance In metallurgy, annealing heats a metal or alloy to a predetermined temperature, holds this temperature for a certain time, and then decreases the metal to room temperature to change the physical and sometimes also the chemical properties of the material. Researchers introduce a similar concept to simulated annealing to predict minimum-energy conformations of biological macromolecules. In this work, we experimentally verify that annealing at a fast cooling rate can synchronize the 70 S ribosome into a nonrotated state with minimum energy in our free-energy landscape analysis. Our results not only offer a facile yet robust approach to stabilizing proteins for high-resolution structural analysis but also contribute to understanding of protein folding and temperature adaptation.