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Updated: Jan 8, 2026

Following the Dynamics of Structural Variants in Experimentally Evolved Populations
Published on: February 3, 2023
On the Variation of Structural Divergence Among Residues in Enzyme Evolution.
Julian Echave1, Mathilde Carpentier2
1Instituto de Ciencias Físicas (ICIFI-CONICET), Universidad Nacional de San Martín, Buenos Aires, Argentina.
Protein structural divergence varies with residue flexibility and distance from the active site. This variation is shaped by both non-functional and functional evolutionary constraints, challenging previous assumptions about enzyme evolution.
Area of Science:
- Evolutionary biology
- Structural biology
- Biochemistry
Background:
- Sequence variation is well-studied, but structural divergence patterns are less understood.
- Protein structural divergence is known to vary among residues.
Purpose of the Study:
- To investigate the factors driving structural divergence in homologous enzymes.
- To understand the interplay between residue flexibility, active site proximity, and evolutionary constraints on protein structure.
Main Methods:
- Comparative analysis of homologous enzyme families.
- Computational modeling to disentangle evolutionary constraints.
- Analysis of residue flexibility and distance from the active site.
Main Results:
- Structural divergence increases with residue flexibility and distance from the active site.
- Two independent evolutionary constraints (non-functional and functional) shape structural divergence patterns.
- Active site conservation is influenced by both functional requirements and inherent rigidity.
Conclusions:
- The relationship between protein dynamics and evolutionary structural variation is not universal.
- Active site conservation is not solely due to functional constraints.
- The balance of non-functional and functional constraints dictates enzyme structural evolution.
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