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Updated: May 31, 2026
06:48
Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
Published on: January 5, 2024
Slow protein evolutionary rates are dictated by surface-core association
Agnes Tóth-Petróczy1, Dan S Tawfik
1Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel.
Summary
Protein evolution rates vary by position. Slow evolution in some proteins is linked to a "frozen" surface, constraining both surface and core residue changes, suggesting protein interactions or stability needs drive this constraint.
Area of Science:
- Evolutionary Biology
- Molecular Biology
- Biophysics
Background:
- Protein evolution rates vary significantly, but the underlying positional constraints are not fully understood.
- Understanding these constraints is crucial for predicting protein function and adaptation.
Purpose of the Study:
- To investigate the positional rates of evolution within proteins.
- To identify factors contributing to exceptionally slow protein evolution.
Main Methods:
- Comparative analysis of evolutionary rates at both protein and residue levels across diverse proteins.
- Statistical analysis of residue evolutionary rates, categorizing them by location (core, surface, disordered) and functional context.
Main Results:
- Most proteins show distinct evolutionary rates for core, surface, and disordered residues.
- A subset of very slowly evolving proteins exhibits an unusually deep peak for core residues (log(2)μ ∼ -4) and a diminished surface peak.
- Accumulation of substitutions in surface residues appears to facilitate core substitutions, while surface constraint can halt core evolution.
Conclusions:
- Protein surface constraints, potentially due to interactions or stability requirements, can significantly slow down core residue evolution.
- The interplay between surface and core residue evolution is critical for determining overall protein evolutionary rates.
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