Scale‐free Spatio‐temporal Correlations in Conformational Fluctuations of Intrinsically Disordered Proteins
Abstract The self‐assembly of intrinsically disordered proteins (IDPs) into condensed phases and the formation of membrane‐less organelles (MLOs) can be considered as the phenomenon of collective behavior. The conformational dynamics of IDPs are essential for their interactions and the formation of...
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Wiley
2025-03-01
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| Series: | Advanced Science |
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| Online Access: | https://doi.org/10.1002/advs.202412989 |
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| author | Haoyu Song Jian Cui Guorong Hu Long Xiong Yanee Wutthinitikornkit Hai Lei Jingyuan Li |
| author_facet | Haoyu Song Jian Cui Guorong Hu Long Xiong Yanee Wutthinitikornkit Hai Lei Jingyuan Li |
| author_sort | Haoyu Song |
| collection | DOAJ |
| description | Abstract The self‐assembly of intrinsically disordered proteins (IDPs) into condensed phases and the formation of membrane‐less organelles (MLOs) can be considered as the phenomenon of collective behavior. The conformational dynamics of IDPs are essential for their interactions and the formation of a condensed phase. From a physical perspective, collective behavior and the emergence of phase are associated with long‐range correlations. Here the conformational dynamics of IDPs and the correlations therein are analyzed, using µs‐scale atomistic molecular dynamics (MD) simulations and single‐molecule Förster resonance energy transfer (smFRET) experiments. The existence of typical scale‐free spatio‐temporal correlations in IDP conformational fluctuations is demonstrated. Their conformational evolutions exhibit “1/f noise” power spectra and are accompanied by the appearance of residue domains following a power‐law size distribution. Additionally, the motions of residues present scale‐free behavioral correlation. These scale‐free correlations resemble those in physical systems near critical points, suggesting that IDPs are poised at a critical state. Therefore, IDPs can effectively respond to finite differences in sequence compositions and engender considerable structural heterogeneity which is beneficial for IDP interactions and phase formation. |
| format | Article |
| id | doaj-art-423fffae5e5c4f959c01351f9f452bee |
| institution | Kabale University |
| issn | 2198-3844 |
| language | English |
| publishDate | 2025-03-01 |
| publisher | Wiley |
| record_format | Article |
| series | Advanced Science |
| spelling | doaj-art-423fffae5e5c4f959c01351f9f452bee2025-08-20T03:27:46ZengWileyAdvanced Science2198-38442025-03-01129n/an/a10.1002/advs.202412989Scale‐free Spatio‐temporal Correlations in Conformational Fluctuations of Intrinsically Disordered ProteinsHaoyu Song0Jian Cui1Guorong Hu2Long Xiong3Yanee Wutthinitikornkit4Hai Lei5Jingyuan Li6School of Physics Zhejiang University Hangzhou 310058 PR ChinaCollaborative Innovation Center of Advanced Microstructures National Laboratory of Solid State Microstructure Department of Physics Nanjing University Nanjing 210093 PR ChinaSchool of Physics Zhejiang University Hangzhou 310058 PR ChinaSchool of Physics and Astronomy Yunnan University Kunming 650091 PR ChinaSchool of Physics Zhejiang University Hangzhou 310058 PR ChinaSchool of Physics Zhejiang University Hangzhou 310058 PR ChinaSchool of Physics Zhejiang University Hangzhou 310058 PR ChinaAbstract The self‐assembly of intrinsically disordered proteins (IDPs) into condensed phases and the formation of membrane‐less organelles (MLOs) can be considered as the phenomenon of collective behavior. The conformational dynamics of IDPs are essential for their interactions and the formation of a condensed phase. From a physical perspective, collective behavior and the emergence of phase are associated with long‐range correlations. Here the conformational dynamics of IDPs and the correlations therein are analyzed, using µs‐scale atomistic molecular dynamics (MD) simulations and single‐molecule Förster resonance energy transfer (smFRET) experiments. The existence of typical scale‐free spatio‐temporal correlations in IDP conformational fluctuations is demonstrated. Their conformational evolutions exhibit “1/f noise” power spectra and are accompanied by the appearance of residue domains following a power‐law size distribution. Additionally, the motions of residues present scale‐free behavioral correlation. These scale‐free correlations resemble those in physical systems near critical points, suggesting that IDPs are poised at a critical state. Therefore, IDPs can effectively respond to finite differences in sequence compositions and engender considerable structural heterogeneity which is beneficial for IDP interactions and phase formation.https://doi.org/10.1002/advs.202412989collective behaviorconformational dynamicscritical phenomenaintrinsically disordered proteinsscale‐free correlation |
| spellingShingle | Haoyu Song Jian Cui Guorong Hu Long Xiong Yanee Wutthinitikornkit Hai Lei Jingyuan Li Scale‐free Spatio‐temporal Correlations in Conformational Fluctuations of Intrinsically Disordered Proteins Advanced Science collective behavior conformational dynamics critical phenomena intrinsically disordered proteins scale‐free correlation |
| title | Scale‐free Spatio‐temporal Correlations in Conformational Fluctuations of Intrinsically Disordered Proteins |
| title_full | Scale‐free Spatio‐temporal Correlations in Conformational Fluctuations of Intrinsically Disordered Proteins |
| title_fullStr | Scale‐free Spatio‐temporal Correlations in Conformational Fluctuations of Intrinsically Disordered Proteins |
| title_full_unstemmed | Scale‐free Spatio‐temporal Correlations in Conformational Fluctuations of Intrinsically Disordered Proteins |
| title_short | Scale‐free Spatio‐temporal Correlations in Conformational Fluctuations of Intrinsically Disordered Proteins |
| title_sort | scale free spatio temporal correlations in conformational fluctuations of intrinsically disordered proteins |
| topic | collective behavior conformational dynamics critical phenomena intrinsically disordered proteins scale‐free correlation |
| url | https://doi.org/10.1002/advs.202412989 |
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