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Related Experiment Video

Updated: May 23, 2026

Fabrication of Three-Dimensional Graphene-Based Polyhedrons via Origami-Like Self-Folding
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Folding without charges.

Martin Kurnik1, Linda Hedberg, Jens Danielsson

  • 1Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden.

Proceedings of the National Academy of Sciences of the United States of America
|March 29, 2012
PubMed
Summary
This summary is machine-generated.

Removing side-chain charges from protein S6 did not disrupt its structure or folding. Surprisingly, the charge-depleted protein folded faster, but showed increased aggregation over time, revealing distinct codes for protein folding and intermolecular interactions.

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Area of Science:

  • Protein biochemistry
  • Structural biology
  • Biophysics

Background:

  • Protein surface charges act as
  • structural gatekeepers
  • preventing unwanted interactions like aggregation and binding.

Purpose of the Study:

  • Investigate if side-chain charges, despite desolvation costs, prevent misfolded protein traps during folding.
  • Determine the role of charge in protein S6 folding and structural stability.

Main Methods:

  • Systematic removal of all 32 side-chain charges from the 101-residue protein S6 (Thermus thermophilus).
  • Comparative analysis of folding transitions, structural integrity, folding kinetics, and aggregation propensity between wild-type and charge-depleted S6 variants.

Main Results:

  • The charge-depleted S6 variant maintained native structure and cooperative folding.
  • Folding kinetics were accelerated in the absence of side-chain charges compared to wild-type.
  • Charge removal led to significant protein aggregation on longer timescales.

Conclusions:

  • Protein S6's native contact bias is charge-independent, governed by hydrophobic packing and hydrogen bonds.
  • Protein folding specificity relies on non-charge interactions, while solubility and binding critically depend on side-chain charges.