Non-equilibrium thermodynamics of molecular evolution

Area of Science:

• Evolutionary biology
• Bioinformatics
• Statistical mechanics

Background:

• Investigating the information complexity of protein sequences is crucial for understanding evolutionary processes.
• Previous studies have explored sequence evolution through various theoretical and empirical lenses.

Purpose of the Study:

• To investigate the information complexity evolution in a large protein sequence database.
• To determine the rate of change in information entropy over evolutionary time.
• To link sequence information to protein structure thermodynamics and molecular evolution models.

Main Methods:

• Calculating information entropy based on algorithmic complexity of protein sequences.
• Analyzing a large database of protein sequences to track changes over evolutionary time.
• Applying statistical mechanical theory to interpret sequence information and thermodynamics.

Main Results:

• Information entropy changes at a constant rate with evolutionary time.
• Conserved residues have higher information content than changed residues, indicating decreased randomness.
• Information content change per amino acid substitution is consistent across studied protein sequences.

Conclusions:

• Sequence evolution is driven towards minimal complexity production and minimum thermodynamic entropy production.
• A statistical mechanical framework explains molecular evolution, integrating neutralist and selectionist aspects.
• The findings provide a physical basis for understanding protein sequence evolution and stability.