Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide
exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the …

Highlights•Proteins begin to fold within the polypeptide exit tunnel of the
ribosome.•Ribosomes change the landscape of protein folding.•Ribosomes can stabilize …

Cellular proteins begin to fold as they emerge from the ribosome. The folding landscape of
nascent chains is not only shaped by their amino acid sequence but also by the interactions …

During protein synthesis, the growing nascent peptide chain moves inside the polypeptide
exit tunnel of the ribosome from the peptidyl transferase center towards the exit port where it …

All cellular proteins are synthesized by the ribosome, an intricate molecular machine that
translates the information of protein coding genes into the amino acid alphabet. The linear …

In the living cells, the folding of many proteins is largely believed to begin co-translationally,
during their biosynthesis at the ribosomes. In the ribosomal tunnel, the nascent peptide may …

Nascent proteins appear to fold co-translationally. The ribosome itself may function as a
chaperone, providing a sheltered environment in which the nascent peptide is protected …

Identifying and understanding the differences between protein folding in bulk solution and in
the cell is a crucial challenge facing biology. Using Langevin dynamics, we have simulated …

Correct folding is a prerequisite for the biological activity of most proteins. Folding has
largely been studied using in vitro refolding assays with isolated small, robustly folding …

Folding of polypeptides begins during their synthesis on ribosomes. This process has
evolved as a means for the cell to maintain proteostasis, by mitigating the risk of protein …