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Published on: October 24, 2025
Intrinsic noise suppression in protein allostery: Quantifying pathway redundancy via spanning tree statistics
1Koc University, Chemical and Biological Engineering, Istanbul, Turkey.
Physical Review. E
|July 24, 2026
Summary
This study introduces a new framework to analyze protein allosteric communication pathways. It reveals how network topology inherently suppresses noise, enhancing signal transmission for robust protein function.
Area of Science:
- Biophysics
- Computational Biology
- Structural Biology
Background:
- Allosteric regulation in proteins relies on collective dynamics across residue contact networks.
- The precise contribution of multiple communication pathways to signal transmission and noise suppression is not fully understood.
Purpose of the Study:
- To develop a quantitative framework for analyzing allosteric communication pathways in proteins.
- To investigate how pathway multiplicity and statistical weighting influence noise suppression and signal transmission.
Main Methods:
- Developed a spanning-tree-based framework to quantify allosteric communication as an ensemble of pathways.
- Introduced a dynamic distance measure linking local perturbations to global network entropy changes.
- Derived exact path probabilities using spanning-tree calculus and compared uniform versus topology-aware descriptions.
Main Results:
- Demonstrated that topology-aware weighting concentrates signal transmission onto dominant, shorter pathways.
- Showed significant variability in path usage, entropy reduction, and signal-to-noise enhancement across different allosteric proteins.
- Identified robustness in allosteric signaling as an emergent property of protein contact topology.
Conclusions:
- The developed framework provides a quantitative link between protein structure, dynamics, and information flow.
- Noise suppression in allosteric communication can be viewed as an intrinsic network topology-driven averaging mechanism.
- The findings suggest that pathway redundancy is crucial for robust allosteric signaling.
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