Single-molecule approaches reveal outer membrane protein biogenesis dynamics

Research output: Contribution to journalResearch articleContributedpeer-review



Outer membrane proteins (OMPs) maintain the viability of Gram-negative bacteria by functioning as receptors, transporters, ion channels, lipases, and porins. Folding and assembly of OMPs involves synchronized action of chaperones and multi-protein machineries which escort the highly hydrophobic polypeptides to their target outer membrane in a folding competent state. Previous studies have identified proteins and their involvement along the OMP biogenesis pathway. Yet, the mechanisms of action and the intriguing ability of all these molecular machines to work without the typical cellular energy source of ATP, but solely based on thermodynamic principles, are still not well understood. Here, we highlight how different single-molecule studies can shed additional light on the mechanisms and kinetics of OMP biogenesis.


Original languageEnglish
Article number2200149
Issue number12
Early online date25 Oct 2022
Publication statusPublished - Dec 2022

External IDs

Scopus 85140382765
Mendeley dc21d082-2f12-37e3-b719-5f707d91d499
ORCID /0000-0002-6209-2364/work/142237701
ORCID /0000-0002-4657-9092/work/142247777



  • AFM, BAM, FCS, OMP biogenesis, SecYEG, Skp, SurA, dynamics, single-molecule FRET

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