Catalyzing Protein Folding by Chaperones

Protein folding is a fundamental process essential for cellular growth and health, yet it is also susceptible to errors that can result in misfolding and disease. This literature review explores the current knowledge of the roles of different factors on protein folding in the cell. We examine the cellular proteostasis network, with a focus on the catalytic actions of prolyl isomerases and molecular chaperones (including RNA G-quadruplexes), which collaborate to guide newly synthesized polypeptides toward their native structures and prevent aggregation. By integrating structural and biochemical insights, this review highlights the current understanding and ongoing questions regarding how chaperones can improve folding times of proteins to physiological pertinent rates.