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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
Published on: July 17, 2019
Self-assembly and evolution of homomeric protein complexes
Gabriel Villar1, Alex W Wilber, Alex J Williamson
1Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QZ, United Kingdom.
Physical Review Letters
|April 28, 2009
Summary
A simple patchy particle model explains how protein complex evolution leads to weaker new interactions and stable subcomplexes. This results in hierarchical self-assembly dynamics for dihedral complexes.
Area of Science:
- Biophysics
- Biochemistry
- Computational Biology
Background:
- Homomeric protein complexes are crucial for cellular functions.
- Understanding the thermodynamics and dynamics of their self-assembly is essential.
- Dihedral complexes represent a significant class of protein assemblies.
Purpose of the Study:
- To introduce a simple patchy particle model for studying protein complex self-assembly.
- To rationalize existing experimental findings for dihedral complexes.
- To elucidate the evolutionary principles governing protein-protein interactions and assembly dynamics.
Main Methods:
- Development of a coarse-grained patchy particle model.
- Thermodynamic calculations to assess stability.
- Dynamic simulations to analyze assembly pathways.
- Analysis of interaction strengths and subcomplex formation.
Main Results:
- The model successfully rationalizes experimental observations for dihedral complexes.
- Evolution favors weaker, newer interactions while retaining stability in stronger, older interactions.
- Thermodynamically stable subcomplexes emerge upon destabilization of protein-protein interactions.
- Hierarchical self-assembly dynamics are observed with stable subcomplexes as kinetic intermediates.
Conclusions:
- The patchy particle model provides a robust framework for understanding protein complex self-assembly.
- Evolutionary pressures naturally guide systems towards specific interaction landscapes.
- The findings offer insights into the design principles of stable and dynamically controlled protein assemblies.
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