Many-body effect renders universal subdiffusion to water on different proteins
Diffusion of interfacial water is crucial for the function and stability of enclosed protein molecule. By combining neutron scattering and molecular dynamics simulation results, we found that the interfacial water on different proteins including intrinsically disordered proteins exhibit a universal...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
American Physical Society
2022-04-01
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| Series: | Physical Review Research |
| Online Access: | http://doi.org/10.1103/PhysRevResearch.4.L022003 |
| _version_ | 1797210830124613632 |
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| author | Song Li Pan Tan Jun Li Min Tang Liang Hong |
| author_facet | Song Li Pan Tan Jun Li Min Tang Liang Hong |
| author_sort | Song Li |
| collection | DOAJ |
| description | Diffusion of interfacial water is crucial for the function and stability of enclosed protein molecule. By combining neutron scattering and molecular dynamics simulation results, we found that the interfacial water on different proteins including intrinsically disordered proteins exhibit a universal subdiffusive motion with a common power law. Further analysis of the simulation trajectories and analytical modeling reveal that it is the many-body effect, i.e., water prefers to jump between shallow trapping sites on the protein as the deep ones are mostly occupied, that overrides the surface differences among proteins to render the interfacial water universal subdiffusion. |
| first_indexed | 2024-04-24T10:16:49Z |
| format | Article |
| id | doaj.art-f6d45ed8fb264fe1b81abb5a5e791dda |
| institution | Directory Open Access Journal |
| issn | 2643-1564 |
| language | English |
| last_indexed | 2024-04-24T10:16:49Z |
| publishDate | 2022-04-01 |
| publisher | American Physical Society |
| record_format | Article |
| series | Physical Review Research |
| spelling | doaj.art-f6d45ed8fb264fe1b81abb5a5e791dda2024-04-12T17:19:37ZengAmerican Physical SocietyPhysical Review Research2643-15642022-04-0142L02200310.1103/PhysRevResearch.4.L022003Many-body effect renders universal subdiffusion to water on different proteinsSong LiPan TanJun LiMin TangLiang HongDiffusion of interfacial water is crucial for the function and stability of enclosed protein molecule. By combining neutron scattering and molecular dynamics simulation results, we found that the interfacial water on different proteins including intrinsically disordered proteins exhibit a universal subdiffusive motion with a common power law. Further analysis of the simulation trajectories and analytical modeling reveal that it is the many-body effect, i.e., water prefers to jump between shallow trapping sites on the protein as the deep ones are mostly occupied, that overrides the surface differences among proteins to render the interfacial water universal subdiffusion.http://doi.org/10.1103/PhysRevResearch.4.L022003 |
| spellingShingle | Song Li Pan Tan Jun Li Min Tang Liang Hong Many-body effect renders universal subdiffusion to water on different proteins Physical Review Research |
| title | Many-body effect renders universal subdiffusion to water on different proteins |
| title_full | Many-body effect renders universal subdiffusion to water on different proteins |
| title_fullStr | Many-body effect renders universal subdiffusion to water on different proteins |
| title_full_unstemmed | Many-body effect renders universal subdiffusion to water on different proteins |
| title_short | Many-body effect renders universal subdiffusion to water on different proteins |
| title_sort | many body effect renders universal subdiffusion to water on different proteins |
| url | http://doi.org/10.1103/PhysRevResearch.4.L022003 |
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