The Sec61 or SecY channel, a universally conserved protein-conducting channel,
translocates proteins across and integrates proteins into the eukaryotic endoplasmic …

Cells face a constant challenge as they produce new proteins. The newly synthesized
polypeptides must be folded properly to avoid aggregation. If proteins do misfold, they must …

The choice of codons can influence local translation kinetics during protein synthesis.
Whether codon preference is linked to cotranslational regulation of polypeptide folding …

Membrane proteins are inserted into the endoplasmic reticulum (ER) by two highly
conserved parallel pathways. The well-studied co-translational pathway uses signal …

Co-translational protein targeting to the endoplasmic reticulum (ER), represents an
evolutionary-conserved mechanism to target proteins into the secretory pathway. In this …

Highlights•Co-translational folding is influenced by translational pausing mechanisms.•The
ribosome is providing a folding environment for nascent chains.•Action of nascent chain …

During the last five decades, studies of protein folding in dilute buffer solutions have
produced a rich picture of this complex process. In the cell, however, proteins can start to …

Protein trafficking and localization in plastids involve a complex interplay between ancient
(prokaryotic) and novel (eukaryotic) translocases and targeting machineries. During …

Integral membrane proteins are assembled into the ER membrane via a continuous
ribosome-translocon channel. The hydrophobicity and thickness of the core of the …

Chaperones, which assist protein folding are essential components of every living cell. The
yeast ribosome-associated complex (RAC) is a chaperone that is highly conserved in …