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Area of Science:

  • Protein engineering and biophysics
  • Computational biology and structural biology

Background:

  • Natural proteins exhibit complex, unique folding pathways.
  • Designed coiled-coil protein origami (CCPO) cages differ from natural proteins, with folds dictated by long-range interactions between coiled-coil (CC) modules in a single chain.

Purpose of the Study:

  • To investigate the folding pathway of CCPO proteins.
  • To demonstrate a stepwise sequential folding mechanism in CCPO.
  • To explore the implications for simplifying CCPO design.

Main Methods:

  • Utilized molecular dynamics simulations to model protein folding.
  • Employed stopped-flow Förster resonance energy transfer (FRET) measurements for experimental validation.

Main Results:

  • CCPO proteins fold via a stepwise sequential pathway.
  • Folding is governed by the intra-chain distance between CC modules.
  • The number of distinct CC modules for a CCPO tetrahedron can be reduced from six to three.

Conclusions:

  • The stepwise, modular folding of CCPO offers insights into tandem repeat protein folding.
  • This folding mechanism can be leveraged to design modular protein structures.
  • CCPO design requirements are relaxed due to the ability to reuse identical CC modules.