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Updated: Feb 12, 2026

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Fodis: Software for Protein Unfolding Analysis.

Nicola Galvanetto1, Andrea Perissinotto1, Andrea Pedroni1

  • 1International School for Advanced Studies (SISSA), Trieste, Italy.

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|March 29, 2018
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Summary

A new open-source tool, Fodis, standardizes protein folding analysis from single-molecule force spectroscopy data. It automates processing and classifies unfolding pathways and structural heterogeneity.

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Area of Science:

  • Biophysics
  • Biochemistry
  • Molecular Biology

Background:

  • Single-molecule force spectroscopy (SMFS) has been used for 20 years to study protein folding dynamics.
  • A lack of standardized methods hinders data analysis and sharing within the scientific community.

Purpose of the Study:

  • To develop an open-source tool for standardized analysis of SMFS data.
  • To provide automated processing, analysis, and classification of force-distance curves.
  • To classify protein unfolding pathways and identify structural heterogeneity.

Main Methods:

  • Development of an open-source software tool named Fodis.
  • Application of Fodis to analyze force-distance curves from SMFS experiments.
  • Implementation of automated data processing and classification algorithms.

Main Results:

  • Fodis enables almost automatic processing and analysis of SMFS data.
  • The tool classifies force-distance curves, revealing protein unfolding pathways.
  • Structural heterogeneity during protein unfolding is identified and classified.

Conclusions:

  • Fodis offers a standardized and automated approach for SMFS data analysis.
  • The tool facilitates the study of protein folding dynamics and heterogeneity.
  • Fodis promotes data sharing and reproducibility in the field.