A global search for extracytoplasmic folding catalysts in Escherichia coli was undertaken
using different genetic systems that produce unstable or misfolded proteins in the periplasm. …

Protein export is an essential mechanism in living cells and exported proteins are usually
translocated through a protein-conducting channel in an unfolded state. Here we analyze, by …

We report experimentally the dynamic properties of the entry and transport of unfolded and
native proteins through a solid-state nanopore as a function of applied voltage, and we …

Two-component systems reprogramme diverse aspects of microbial physiology in response
to environmental cues. Canonical systems are composed of a transmembrane sensor …

Proteins subjected to an electric field and forced to pass through a nanopore induce blockades
of ionic current that depend on the protein and nanopore characteristics and interactions …

The nature of molecular chaperones in the periplasm of Escherichia coli that assist newly
translocated proteins to reach their native state has remained poorly defined. Here, we show …

The nanopore technique has great potential to discriminate conformations of proteins. It is a
very interesting system to mimic and understand the process of translocation of …

We report experimentally the transport of an unfolded protein through a narrow solid-state
nanopore of 3 nm diameter as a function of applied voltage. The random coil polypeptide …

Understanding protein folding remains a challenge. A difficulty is to investigate
experimentally all the conformations in the energy landscape. Only single molecule methods, …

We have investigated the possibility of cell-fee synthesis of membrane proteins in the
absence of a membrane and in the presence of detergent. We used the bacterial …