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 misfolding …

Although detailed pictures of ribosome structures are emerging, little is known about the
structural and cotranslational folding properties of nascent polypeptide chains at the atomic level…

Co-translational folding is crucial to ensure the production of biologically active proteins.
The ribosome can alter the folding pathways of nascent polypeptide chains, yet a structural …

Co-translational folding is a fundamental process for the efficient biosynthesis of nascent
polypeptides that emerge through the ribosome exit tunnel. To understand how this process is …

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 …

During biosynthesis, proteins can begin folding co-translationally to acquire their biologically-active
structures. Folding, however, is an imperfect process and in many cases misfolding …

During biosynthesis on the ribosome, an elongating nascent polypeptide chain can begin to
fold, in a process that is central to all living systems. Detailed structural studies of co-…

Cotranslational folding (CTF) is a fundamental molecular process that ensures efficient protein
biosynthesis and minimizes the formation of misfolded states. However, the complexity of …

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 …

The folding of many proteins can begin during biosynthesis on the ribosome and can be
modulated by the ribosome itself. Such perturbations are generally believed to be mediated …