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Detecting selection on protein stability through statistical mechanical models of folding and evolution
1Centro de Biologia Molecular Severo Ochoa, CSIC-UAM, Madrid E-28049, Spain. ubastolla@cbm.csic.es.
Biomolecules
|June 28, 2014
Summary
Physics and evolution synergize to explain biomolecule properties. This review integrates both to detect selection on protein stability and dynamics, revealing evolutionary trade-offs in protein design.
Area of Science:
- Biophysics
- Molecular Evolution
- Protein Thermodynamics
Background:
- Biomolecule properties arise from physics and evolution.
- Protein thermodynamics relies on statistical mechanics of structures.
- Molecular evolution parallels statistical mechanics of sequences.
Purpose of the Study:
- Integrate physics and evolutionary viewpoints.
- Detect selection on protein folded state stability.
- Rationalize physical properties of biomolecules.
Main Methods:
- Statistical mechanics in protein structure space.
- Statistical mechanics in protein sequence space.
- Analysis of positive and negative design principles.
Main Results:
- Positive design enhances folded state stability.
- Negative design destabilizes misfolded conformations.
- Evolution balances folding rate and stability via trade-offs.
Conclusions:
- Selection optimizes protein stability and dynamics.
- Protein length influences stability and design.
- Functional movements are accelerated by selection on dynamics.
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