Frustration, dynamics and catalysis
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arXiv
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| Main Authors: | , |
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| Format: | Preprint |
| Published: |
2025
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| _version_ | 1866911043938156544 |
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| author | Parra, R. Gonzalo Ferreiro, Diego U. |
| author_facet | Parra, R. Gonzalo Ferreiro, Diego U. |
| contents | The controlled dissipation of chemical potentials is the fundamental way cells make a living. Enzyme-mediated catalysis allows the various transformations to proceed at biologically relevant rates with remarkable precision and efficiency. Theory, experiments and computational studies coincide to show that local frustration is a useful concept to relate protein dynamics with catalytic power. Local frustration gives rise to the asperities of the energy landscapes that can harness the thermal fluctuations to guide the functional protein motions. We review here recent advances into these relationships from various fields of protein science. The biologically relevant dynamics is tuned by the evolution of protein sequences that modulate the local frustration patterns to near optimal values. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2505_00600 |
| institution | arXiv |
| publishDate | 2025 |
| record_format | arxiv |
| spellingShingle | Frustration, dynamics and catalysis Parra, R. Gonzalo Ferreiro, Diego U. Biomolecules Soft Condensed Matter Biological Physics The controlled dissipation of chemical potentials is the fundamental way cells make a living. Enzyme-mediated catalysis allows the various transformations to proceed at biologically relevant rates with remarkable precision and efficiency. Theory, experiments and computational studies coincide to show that local frustration is a useful concept to relate protein dynamics with catalytic power. Local frustration gives rise to the asperities of the energy landscapes that can harness the thermal fluctuations to guide the functional protein motions. We review here recent advances into these relationships from various fields of protein science. The biologically relevant dynamics is tuned by the evolution of protein sequences that modulate the local frustration patterns to near optimal values. |
| title | Frustration, dynamics and catalysis |
| topic | Biomolecules Soft Condensed Matter Biological Physics |
| url | https://arxiv.org/abs/2505.00600 |