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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.
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T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
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Tracking Protein Misfolding and Oligomerization: A Temperature-Controlled Ion Mobility-Mass Spectrometry Approach.

Despoina Svingou1, Luke McAlary2, Julian Alexander Harrison1

  • 1Laboratory of Organic Chemistry, Department of Chemistry and Applied Biosciences, ETH Zurich, Zurich, 8093 Switzerland.

Analytical Chemistry
|May 13, 2026
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Summary

Researchers developed a new method using temperature-controlled nanoelectrospray ionization (TC-nESI) and ion mobility-mass spectrometry (IM-MS) to study protein misfolding and oligomerization in neurodegenerative diseases like ALS.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Aberrant protein oligomerization is central to neurodegenerative disorders.
  • Early aggregation intermediates are difficult to study with existing structural techniques.
  • Understanding protein unfolding and early assembly is crucial for disease mechanism investigation.

Purpose of the Study:

  • To develop and validate a methodology for characterizing protein misfolding and oligomerization.
  • To investigate the early aggregation landscape of bovine Cu/Zn superoxide dismutase (SOD1).
  • To elucidate the molecular mechanisms underlying protein aggregation in neurodegenerative diseases.

Main Methods:

  • Temperature-controlled nanoelectrospray ionization (TC-nESI) coupled with high-resolution ion mobility-mass spectrometry (IM-MS).
  • Surface-induced dissociation (SID) and limited proteolysis were employed.
  • Integrative approach to capture transient, low-abundance oligomeric intermediates.

Main Results:

  • TC-nESI-IM-MS successfully detected coexisting misfolded intermediates and soluble oligomers of SOD1.
  • Both holo- and apo-SOD1 undergo dissociation, misfolding, and assembly into heterogeneous oligomers.
  • Specific protein regions (loops V, VI, VII, C-terminus) were identified as key for oligomer interface formation.

Conclusions:

  • The developed TC-nESI-IM-MS platform can temporally and structurally resolve protein misfolding transitions and oligomeric populations.
  • This approach provides a framework for dissecting oligomerization pathways relevant to neurodegenerative diseases.
  • The study reveals a mechanistically rich model for early protein aggregation in SOD1.