Protein folding as a jamming transition
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arXiv
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| Main Authors: | , , , , |
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| Format: | Preprint |
| Published: |
2024
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| Subjects: | |
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| _version_ | 1866909554255593472 |
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| author | Grigas, Alex T. Liu, Zhuoyi Logan, Jack A. Shattuck, Mark D. O'Hern, Corey S. |
| author_facet | Grigas, Alex T. Liu, Zhuoyi Logan, Jack A. Shattuck, Mark D. O'Hern, Corey S. |
| contents | Proteins fold to a specific functional conformation with a densely packed hydrophobic core that controls their stability. We develop a geometric, yet all-atom model for proteins that explains the universal core packing fraction of $ϕ_c=0.55$ found in experimental measurements. We show that as the hydrophobic interactions increase relative to the temperature, a novel jamming transition occurs when the core packing fraction exceeds $ϕ_c$. The model also recapitulates the global structure of proteins since it can accurately refold to native-like structures from partially unfolded states. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2405_09646 |
| institution | arXiv |
| publishDate | 2024 |
| record_format | arxiv |
| spellingShingle | Protein folding as a jamming transition Grigas, Alex T. Liu, Zhuoyi Logan, Jack A. Shattuck, Mark D. O'Hern, Corey S. Soft Condensed Matter Biological Physics Proteins fold to a specific functional conformation with a densely packed hydrophobic core that controls their stability. We develop a geometric, yet all-atom model for proteins that explains the universal core packing fraction of $ϕ_c=0.55$ found in experimental measurements. We show that as the hydrophobic interactions increase relative to the temperature, a novel jamming transition occurs when the core packing fraction exceeds $ϕ_c$. The model also recapitulates the global structure of proteins since it can accurately refold to native-like structures from partially unfolded states. |
| title | Protein folding as a jamming transition |
| topic | Soft Condensed Matter Biological Physics |
| url | https://arxiv.org/abs/2405.09646 |