Optical tweezers have become the method of choice in single-molecule manipulation
studies. In this Primer, we first review the physical principles of optical tweezers and the …

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 …

The use of force probes to induce unfolding and refolding of single molecules through the
application of mechanical tension, known as single-molecule force spectroscopy (SMFS) …

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 …

Multi-domain proteins, containing several structural units within a single polypeptide,
constitute a large fraction of all proteomes. Co-translational folding is assumed to simplify …

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 …

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 …

Nascent polypeptides begin to fold in the constrained space of the ribosomal peptide exit
tunnel. Here we use force-profile analysis (FPA) and photo-induced energy-transfer …