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Related Concept Videos

Studying the Cytoskeleton01:17

Studying the Cytoskeleton

The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
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Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
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Related Experiment Video

Updated: May 29, 2026

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
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Monitoring Membrane Protein Folding Assisted by Insertases and Translocases Using AFM-Based Single-Molecule Force

Tetiana Serdiuk1, Johannes Thoma2, Daniel J Müller3

  • 1Institute of Molecular Systems Biology, ETH Zürich, Otto-Stern-Weg 3, 8093 Zürich, Switzerland.

Chemical Reviews
|May 27, 2026
PubMed
Summary
This summary is machine-generated.

Single-molecule force spectroscopy (SMFS) reveals how membrane proteins fold and insert into cellular membranes. This technique monitors protein folding pathways, aided by insertases, translocases, and chaperones, and detects misfolding.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Membrane Protein Biochemistry

Background:

  • Membrane proteins are crucial for cellular function but challenging to study.
  • Understanding their folding and insertion pathways is vital for deciphering cellular mechanisms.

Purpose of the Study:

  • To review the application of atomic force microscopy-based single-molecule force spectroscopy (SMFS) for studying membrane protein folding.
  • To compare assisted versus unassisted folding pathways of prokaryotic membrane proteins.
  • To highlight SMFS's ability to detect misfolded proteins and the roles of cellular machinery.

Main Methods:

  • Atomic force microscopy (AFM)-based single-molecule force spectroscopy (SMFS).
  • Monitoring unfolding and folding pathways of individual membrane proteins.
  • Studying insertion and folding assisted by insertases, translocases, and chaperones.
  • Utilizing native outer membrane vesicles for studying β-barrel protein folding.

Main Results:

  • SMFS can detect misfolding induced by lipid composition or unassisted folding.
  • Chaperones, insertases (like YidC), and translocases (like SecYEG) assist membrane protein folding and insertion.
  • SecYEG sequentially inserts α-helices, while YidC inserts segments randomly; SecYEG dominates when acting together.
  • The β-barrel assembly machinery (BAM) complex facilitates outer membrane protein folding.

Conclusions:

  • SMFS is a powerful tool for dissecting complex membrane protein insertion and folding mechanisms.
  • Cellular machinery plays critical roles in ensuring proper membrane protein folding and function.
  • Studying proteins in native-like environments enhances understanding of in vivo processes.