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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
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Implications of protein polymorphism on protein phase behaviour.
1Applied Physics, Eindhoven University of Technology, Eindhoven, 5600 MB, The Netherlands. j.stegen@tue.nl.
Soft Matter
|January 29, 2015
Summary
Protein phase behavior is complex, with conformational changes impacting models. This study introduces a two-state model revealing re-entrant phase behavior and distinct condensation mechanisms for native and non-native protein states.
Area of Science:
- Protein biophysics
- Phase transitions
- Supramolecular assembly
Background:
- Protein phase behavior is often simplified using spherical particle models.
- Environmental changes can alter protein conformation, invalidating fixed-structure approximations.
Purpose of the Study:
- To present a two-state model accounting for protein conformational changes during phase separation.
- To investigate the complex phase behavior arising from non-conserved protein conformation.
Main Methods:
- Development of a simple two-state model for protein conformation.
- Analysis of phase behavior including re-entrance and conformational transitioning.
- Investigation of condensation kinetics based on protein pre-condensation conformation.
Main Results:
- The model exhibits complex, non-universal phase behavior with re-entrance.
- A demarcation exists between regimes where conformational change is enslaved by phase separation and where it is independent.
- Condensation in the latter regime requires nucleation of non-native protein clusters.
Conclusions:
- Protein conformational flexibility significantly influences phase behavior.
- Distinguishes between common phase separation and nucleated assembly of non-native aggregates.
- Model supports understanding of protein aggregation mechanisms.
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