Protein folding as a jamming transition
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 $\phi_c=0.55$ found in experimental measurements. We show that as the...
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15-05-2024
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Abstract | 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 $\phi_c=0.55$ 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 $\phi_c$. The model
also recapitulates the global structure of proteins since it can accurately
refold to native-like structures from partially unfolded states. |
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AbstractList | 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 $\phi_c=0.55$ 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 $\phi_c$. The model
also recapitulates the global structure of proteins since it can accurately
refold to native-like structures from partially unfolded states. |
Author | Logan, Jack A Grigas, Alex T O'Hern, Corey S Liu, Zhuoyi Shattuck, Mark D |
Author_xml | – sequence: 1 givenname: Alex T surname: Grigas fullname: Grigas, Alex T – sequence: 2 givenname: Zhuoyi surname: Liu fullname: Liu, Zhuoyi – sequence: 3 givenname: Jack A surname: Logan fullname: Logan, Jack A – sequence: 4 givenname: Mark D surname: Shattuck fullname: Shattuck, Mark D – sequence: 5 givenname: Corey S surname: O'Hern fullname: O'Hern, Corey S |
BackLink | https://doi.org/10.48550/arXiv.2405.09646$$DView paper in arXiv |
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Copyright | http://creativecommons.org/licenses/by/4.0 |
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Snippet | Proteins fold to a specific functional conformation with a densely packed
hydrophobic core that controls their stability. We develop a geometric, yet
all-atom... |
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SourceType | Open Access Repository |
SubjectTerms | Physics - Biological Physics Physics - Soft Condensed Matter |
Title | Protein folding as a jamming transition |
URI | https://arxiv.org/abs/2405.09646 |
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