At what point during translation do proteins fold? It is well established that proteins can fold
cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit …

Membrane proteins destined for insertion into the inner membrane of bacteria or the
endoplasmic reticulum membrane in eukaryotic cells are synthesized by ribosomes bound to the …

While there has been considerable progress in designing protein–protein interactions, the
design of proteins that bind polar surfaces is an unmet challenge. We describe the …

10.7554/eLife.25642.001 Interaction between the nascent polypeptide chain and the ribosomal
exit tunnel can modulate the rate of translation and induce translational arrest to regulate …

On average, every fifth residue in secretory proteins carries either a positive or a negative
charge. In a bacterium such as Escherichia coli, charged residues are exposed to an electric …

Translational arrest peptides (APs) are short stretches of polypeptides that induce
translational stalling when synthesized on a ribosome. Mechanical pulling forces acting on the …

During ribosomal translation, nascent polypeptide chains (NCs) undergo a variety of physical
processes that determine their fate in the cell. This study utilizes a combination of arrest …

In Gram-negative bacteria, periplasmic domains in inner membrane proteins are cotranslationally
translocated across the inner membrane through the SecYEG translocon. To what …

In Gram-negative bacteria, periplasmic domains in inner membrane proteins are cotranslationally
translocated across the inner membrane through the SecYEG translocon. To what …

The biosynthesis of proteins occurs at the ribosomes, where amino acids are linked together
into linear chains. Nascent protein chains may undergo several different processes during …