# Catalyzing Protein Folding by Chaperones

## TL;DR

This review explains how cells use chaperones to help proteins fold correctly, which is crucial for cell function and preventing disease.

## Contribution

The paper provides an updated overview of the proteostasis network, emphasizing the catalytic roles of prolyl isomerases and chaperones in protein folding.

## Key findings

- Molecular chaperones and prolyl isomerases work together to guide proteins into their correct folded states.
- RNA G-quadruplexes are identified as potential contributors to the chaperone network.
- Chaperones can significantly reduce protein folding times to biologically relevant rates.

## Abstract

The thousands of different proteins in our cells must fold into intricate three-dimensional shapes to function properly. Aiding proteins to achieve this correct folded state and maintaining that shape over time is a major challenge to the cell, and failure to do so can have disastrous consequences including many diseases. This review article offers background and up-to-date information on how cells aid proteins to achieve their correctly folded states on timescales that allow life to proceed.

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.