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Reversible switching between two common protein folds in a designed system using only temperature.

Tsega L Solomon1,2, Yanan He1, Nese Sari1

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Researchers designed a protein that reversibly switches between two common folds using only temperature changes. This protein fold switching, controlled by temperature, could enable new protein designs and computational studies.

Keywords:
NMRmetamorphic proteinsprotein designprotein fold switchingprotein structure and dynamics

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Area of Science:

  • Protein engineering
  • Biophysics
  • Structural biology

Background:

  • Naturally occurring metamorphic proteins can change between folded states.
  • Environmental changes or mutations can trigger these protein fold switches.

Purpose of the Study:

  • To demonstrate reversible switching between two common protein folds using only temperature.
  • To engineer a protein system that responds to environmental triggers.

Main Methods:

  • Designed a protein system with a single V90T amino acid substitution.
  • Utilized temperature changes (5°C and 30°C) to induce and observe fold switching.
  • Analyzed protein structure, dynamics, and interconversion energetics/kinetics.

Main Results:

  • A latent 3α state was unmasked from an α/β-plait topology.
  • The protein populated both 3α and α/β-plait forms simultaneously.
  • Fold switching was temperature-dependent, with distinct predominant states at 5°C (3α) and 30°C (α/β-plait).
  • Ligand-binding function was regulated by large structural changes within a biologically relevant temperature range.

Conclusions:

  • A designed protein system can reversibly switch between 3α and α/β-plait topologies using temperature.
  • This fold switching mechanism offers a novel approach for designing environment-responsive proteins.
  • The system serves as a model for studying temperature-dependent protein stability and fold switching computationally.