Protein folding as a jamming transition

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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Bibliographic Details
Main Authors: Grigas, Alex T, Liu, Zhuoyi, Logan, Jack A, Shattuck, Mark D, O'Hern, Corey S
Format: Journal Article
Language:English
Published: 15-05-2024
Subjects:
Physics - Biological Physics
Physics - Soft Condensed Matter
Online Access:Get full text
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Summary: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.
DOI:10.48550/arxiv.2405.09646