The formation of protein complexes is crucial to most biological functions. The cellular
mechanisms governing protein complex biogenesis are not yet well understood, but some …

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 …

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 …

Most proteins begin to fold during biosynthesis on the ribosome. It has been suggested that
interactions between the emerging polypeptide and the ribosome surface might allow the …

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 …

A central challenge in the study of intrinsically disordered proteins is the characterization of
the mechanisms by which they bind their physiological interaction partners. Here, we utilize …

Proteins that exsert physiological functions during being translated have been discovered
from prokaryotes to eukaryotes. These proteins, also called regulatory nascent chains, are …

In the cell, the conformations of nascent polypeptide chains during translation are modulated
by both the ribosome and its associated molecular chaperone, trigger factor. The specific …

Many proteins begin to fold as they are being synthesized by the ribosome. Growing
experimental evidence, supported by new theory, simulation and bioinformatics studies …

Most factors that regulate gene transcription in eukaryotic cells are multimeric, often large,
protein complexes. The understanding of the biogenesis pathways of such large and …