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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

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Related Experiment Video

Updated: May 23, 2026

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
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Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.

Sang Ah Kim1, Seoyoon Kim2, Jaehyun Nam2

  • 1School of Biological Sciences and Institute for Molecular Biology and Genetics, Seoul National University, Seoul 08826, South Korea.

Chemical Reviews
|May 21, 2026
PubMed
Summary

Single-molecule force spectroscopy (SMFS) reveals membrane protein folding pathways by capturing transient states. This high-resolution technique quantifies folding dynamics and energy landscapes for complex biological functions.

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OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
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06:45

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

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Area of Science:

  • Biochemistry and Biophysics
  • Molecular Biology
  • Cell Biology

Background:

  • Membrane proteins are crucial for cellular functions, requiring complex folding within lipid bilayers.
  • Understanding membrane protein folding necessitates observing transient intermediate states often missed by ensemble methods.

Purpose of the Study:

  • To detail the biogenesis of membrane proteins, including targeting, insertion, folding, and oligomerization.
  • To explore how single-molecule force spectroscopy (SMFS) can resolve folding intermediates and energy landscapes.
  • To highlight advanced SMFS techniques for studying membrane protein dynamics and cellular functions.

Main Methods:

  • Single-molecule force spectroscopy (SMFS) to probe membrane protein folding.
  • Analysis of folding trajectories, transition rates, and energy landscapes.
  • Emerging SMFS modalities for oligomerization and in-cell measurements.

Main Results:

  • SMFS provides high-resolution access to membrane protein folding pathways.
  • Transient folding intermediates and their transition rates can be quantified.
  • Advanced SMFS methods link folding dynamics to cellular complexity and function.

Conclusions:

  • SMFS is a powerful tool for deciphering complex membrane protein folding mechanisms.
  • New SMFS approaches integrate molecular folding with cellular biological processes.
  • This research advances the understanding of membrane protein biophysics and function.