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Updated: Jan 8, 2026

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Anomalous proteinaceous shells with octagonal local order.

Sergei B Rochal1, Aleksey S Roshal1, Olga V Konevtsova1

  • 1Southern Federal University, Faculty of Physics, 344090 Rostov-on-Don, Russia.

Physical Review. E
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Summary
This summary is machine-generated.

Protein shells with anomalous structures, unlike typical viral capsids, were identified as octagonal quasicrystals. These findings provide a basis for understanding and applying these novel protein assemblies in biomedicine.

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Area of Science:

  • Structural biology
  • Biophysics
  • Materials science

Background:

  • Protein shells exhibit diverse structures beyond the traditional icosahedral viral capsid model.
  • Anomalous shell structures are crucial for various biomedical applications.

Purpose of the Study:

  • To identify and characterize novel protein shell structures.
  • To develop models for understanding the assembly and properties of these shells.

Main Methods:

  • Exploration of the Protein Data Bank for shell structures.
  • Utilizing the Landau density wave approach for tiling analysis.
  • Simulating non-equilibrium assembly with pair potentials.
  • Minimizing effective elastic energy to reduce tile distortions.

Main Results:

  • Identification of nine types of anomalous shells resembling octagonal quasicrystals.
  • Demonstration that these shells are cubic nets from octagonal tilings.
  • Development of structural models applicable to numerous protein shells, including symmetrical enzymes.

Conclusions:

  • The identified octagonal assemblies represent a new class of protein structures.
  • These findings offer a fundamental basis for future applications and discovery of similar systems.
  • The study bridges concepts from tiling theory, physics, and structural biology.