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Related Concept Videos

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Related Experiment Video

Updated: May 17, 2026

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
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Atomic force microscopy captures folded ribosome bound nascent chains.

Anna Loksztejn1, Zackary Scholl, Piotr E Marszalek

  • 1Department of Mechanical Engineering and Materials Science, Duke University, Durham, North Carolina 27708, USA. al95@duke.edu

Chemical Communications (Cambridge, England)
|October 12, 2012
PubMed
Summary

Direct visualization of protein folding during translation is difficult. This study uses atomic force microscopy (AFM) to capture images of ankyrin-R protein emerging from ribosomes, revealing its initial structure.

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Last Updated: May 17, 2026

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Structural Biology

Background:

  • Direct visualization of co-translational protein folding remains a significant challenge in molecular biology.
  • Understanding how proteins fold as they are synthesized is crucial for cellular function.

Purpose of the Study:

  • To develop and apply a method for visualizing the co-translational folding of large protein constructs.
  • To capture the initial structural conformation of proteins emerging from the ribosome.

Main Methods:

  • Utilized Atomic Force Microscopy (AFM) for high-resolution imaging.
  • Examined large protein constructs based on the membrane binding domain of ankyrin-R.
  • Visualized protein complexes directly associated with ribosomes.

Main Results:

  • Achieved the first direct AFM visualization of large protein constructs co-translationally folding.
  • Captured characteristic "horse-shoe" shape of ankyrin-R as it emerges from the ribosome.
  • Demonstrated the feasibility of imaging nascent polypeptide chains in complex with ribosomes.

Conclusions:

  • AFM provides a powerful tool for studying co-translational protein folding.
  • The study reveals the initial folding pathway of ankyrin-R during its synthesis.
  • This technique opens new avenues for investigating protein biogenesis at the single-molecule level.