Structured Random Binding: a minimal model of protein-protein interactions
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arXiv
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| Format: | Preprint |
| Published: |
2025
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| _version_ | 1866912295377960960 |
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| author | Zou, Ling-Nan |
| author_facet | Zou, Ling-Nan |
| contents | We describe Structured Random Binding (SRB), a minimal model of protein-protein interactions rooted in the statistical physics of disordered systems. In this model, nonspecific binding is a generic consequence of the interaction between random proteins, exhibiting a phase transition from a high temperature state where nonspecific complexes are transient and lack well-defined interaction interfaces, to a low temperature state where the complex structure is frozen and a definite interaction interface is present. Numerically, weakly-bound nonspecific complexes can evolve into tightly-bound, highly specific complexes, but only if the structural correlation length along the peptide backbone is short; moreover, evolved tightly-bound homodimers favor the same interface structure that is predominant in real protein homodimers. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2503_20581 |
| institution | arXiv |
| publishDate | 2025 |
| record_format | arxiv |
| spellingShingle | Structured Random Binding: a minimal model of protein-protein interactions Zou, Ling-Nan Statistical Mechanics Soft Condensed Matter Biological Physics Biomolecules We describe Structured Random Binding (SRB), a minimal model of protein-protein interactions rooted in the statistical physics of disordered systems. In this model, nonspecific binding is a generic consequence of the interaction between random proteins, exhibiting a phase transition from a high temperature state where nonspecific complexes are transient and lack well-defined interaction interfaces, to a low temperature state where the complex structure is frozen and a definite interaction interface is present. Numerically, weakly-bound nonspecific complexes can evolve into tightly-bound, highly specific complexes, but only if the structural correlation length along the peptide backbone is short; moreover, evolved tightly-bound homodimers favor the same interface structure that is predominant in real protein homodimers. |
| title | Structured Random Binding: a minimal model of protein-protein interactions |
| topic | Statistical Mechanics Soft Condensed Matter Biological Physics Biomolecules |
| url | https://arxiv.org/abs/2503.20581 |