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Updated: Feb 10, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
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Extant fold-switching proteins are widespread.

Lauren L Porter1, Loren L Looger2

  • 1Howard Hughes Medical Institute, Janelia Research Campus, Ashburn, VA 20147 porterl@janelia.hhmi.org.

Proceedings of the National Academy of Sciences of the United States of America
|May 23, 2018
PubMed
Summary

Globular proteins can switch folds, challenging the idea of a single 3D structure. This study estimates 0.5-4% of proteins switch folds, revealing they are more common than previously thought.

Keywords:
conformational diversitymetamorphic proteinsprotein fold switchingprotein functionprotein structure

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biophysics

Background:

  • Traditionally, globular proteins are believed to possess a single, stable 3D structure under physiological conditions.
  • Recent research indicates that some proteins can switch between different folds, involving secondary structure remodeling.
  • These fold-switching proteins are categorized as evolved (mutation-induced) or extant (stimulus-induced).

Purpose of the Study:

  • To quantify the frequency of extant fold-switching proteins, previously considered rare.
  • To investigate if the Protein Data Bank (PDB) accurately reflects the prevalence of these proteins.
  • To develop a method for identifying potential fold switchers with limited structural data.

Main Methods:

  • Systematic search of the Protein Data Bank (PDB) to identify known extant fold-switching proteins.
  • Analysis of characteristic features of identified fold switchers, including secondary structure prediction accuracy and folding cooperativity.
  • Application of these features to search the PDB for additional proteins exhibiting signs of structural change but with only one solved conformation.

Main Results:

  • Approximately 100 extant fold-switching proteins were identified in the PDB.
  • Evidence suggests these proteins are widespread, potentially underrepresented in structural databases.
  • An estimated 0.5-4% of proteins in the PDB may undergo fold switching.
  • Dozens of additional putative fold switchers were identified using the developed method.

Conclusions:

  • Extant fold-switching proteins are more prevalent than current structural data suggests.
  • The findings challenge the paradigm of static protein structures and highlight protein plasticity.
  • This prevalence has significant implications for understanding cell biology, genomics, and human health.