Manipulation of individual molecules with optical tweezers provides a powerful means of
interrogating the structure and folding of proteins. Mechanical force is not only a relevant …

Bacteria often encounter temperature fluctuations in their natural habitats and must adapt to
survive. The molecular response of bacteria to sudden temperature upshift or downshift is …

The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

As nascent polypeptides exit ribosomes, they are engaged by a series of processing,
targeting, and folding factors. Here, we present a selective ribosome profiling strategy that …

Cells are faced with the task of folding thousands of different polypeptides into a wide range
of conformations. For many proteins, the folding process requires the action of molecular …

The timely production of functional proteins is of critical importance for the biological activity
of cells. To reach the functional state, newly synthesized polypeptides have to become …

The early events in the life of newly synthesized proteins in the cellular environment are
remarkably complex. Concurrently with their synthesis by the ribosome, nascent …

Introduction Molecular chaperones prevent aggregation and misfolding of proteins in the
cellular environment and are thus central to maintaining protein homeostasis. Molecular …

During ribosome-associated quality control, stalled ribosomes are split into subunits and the
60S-housed nascent polypeptides are poly-ubiquitinated by Listerin. How this low …

During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit
tunnel encounter ribosome-associated chaperones, which assist their folding to the native …