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• W2031609587 abstract "Granular matter is rigid when jammed, and flows under external loads. Here temperature- and force-unfolding molecular dynamics stimulations are used to demonstrate that proteins display features of jamming, characterized by a force distribution peak on folding and a slowdown of stress relaxation. Grains and glasses, widely different materials, arrest their motions upon decreasing temperature and external load, respectively, in common ways, leading to a universal jamming phase diagram conjecture. However, unified theories are lacking, mainly because of the disparate nature of the particle interactions. Here we demonstrate that folded proteins exhibit signatures common to both glassiness and jamming by using temperature- and force-unfolding molecular dynamics simulations. Upon folding, proteins develop a peak in the interatomic force distributions that falls on a universal curve with experimentally measured forces on jammed grains and droplets. Dynamical signatures are found as a dramatic slowdown of stress relaxation upon folding. Together with granular similarities, folding is tied not just to the jamming transition, but a more nuanced picture of anisotropy, preparation protocol and internal interactions emerges. Results have implications for designing stable polymers and can open avenues to link protein folding to jamming theory." @default.
• W2031609587 created "2016-06-24" @default.
• W2031609587 creator A5073866498 @default.
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• W2031609587 date "2012-10-23" @default.
• W2031609587 modified "2023-09-24" @default.
• W2031609587 title "Similarities between protein folding and granular jamming" @default.
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• W2031609587 doi "https://doi.org/10.1038/ncomms2177" @default.
• W2031609587 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3493650" @default.
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• W2031609587 hasPublicationYear "2012" @default.
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