A Unified View of Allostery
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arXiv
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| Hauptverfasser: | , , |
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| Format: | Preprint |
| Veröffentlicht: |
2024
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| _version_ | 1866917835278647296 |
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| author | Rouviere, Eric Rivoire, Olivier Ranganathan, Rama |
| author_facet | Rouviere, Eric Rivoire, Olivier Ranganathan, Rama |
| contents | Allostery is a fundamental property of proteins that represents the functional coupling between distantly located sites. In different manifestations, this property underlies signal transduction, gene expression, and regulation -- elementary reactions in networks comprising cellular information and metabolic processing systems. In this work, we present a reduced theoretical model for allostery that encompasses the many diverse mechanisms described in past work. What emerges is a basic classification of different forms of allostery into two groups: those that couple distant sites through soft normal modes within a single state, and those that possess multiple states, with effective interactions between sites emerging only upon transitioning between these states. This work serves to unify the extensive past theoretical work on the phenomenology and machinery of allostery in proteins. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2411_06519 |
| institution | arXiv |
| publishDate | 2024 |
| record_format | arxiv |
| spellingShingle | A Unified View of Allostery Rouviere, Eric Rivoire, Olivier Ranganathan, Rama Biomolecules Allostery is a fundamental property of proteins that represents the functional coupling between distantly located sites. In different manifestations, this property underlies signal transduction, gene expression, and regulation -- elementary reactions in networks comprising cellular information and metabolic processing systems. In this work, we present a reduced theoretical model for allostery that encompasses the many diverse mechanisms described in past work. What emerges is a basic classification of different forms of allostery into two groups: those that couple distant sites through soft normal modes within a single state, and those that possess multiple states, with effective interactions between sites emerging only upon transitioning between these states. This work serves to unify the extensive past theoretical work on the phenomenology and machinery of allostery in proteins. |
| title | A Unified View of Allostery |
| topic | Biomolecules |
| url | https://arxiv.org/abs/2411.06519 |