Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K
The protein dynamical transition at ~200 K, where the biomolecule transforms from a harmonic, non-functional form to an anharmonic, functional state, has been thought to be slaved to the thermal activation of dynamics in its surface hydration water. Here, by selectively probing the dynamics of prote...
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2024-08-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/95665 |
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| _version_ | 1849738070757212160 |
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| author | Lirong Zheng Bingxin Zhou Banghao Wu Yang Tan Juan Huang Madhusudan Tyagi Victoria García Sakai Takeshi Yamada Hugh O'Neill Qiu Zhang Liang Hong |
| author_facet | Lirong Zheng Bingxin Zhou Banghao Wu Yang Tan Juan Huang Madhusudan Tyagi Victoria García Sakai Takeshi Yamada Hugh O'Neill Qiu Zhang Liang Hong |
| author_sort | Lirong Zheng |
| collection | DOAJ |
| description | The protein dynamical transition at ~200 K, where the biomolecule transforms from a harmonic, non-functional form to an anharmonic, functional state, has been thought to be slaved to the thermal activation of dynamics in its surface hydration water. Here, by selectively probing the dynamics of protein and hydration water using elastic neutron scattering and isotopic labeling, we found that the onset of anharmonicity in the two components around 200 K is decoupled. The one in protein is an intrinsic transition, whose characteristic temperature is independent of the instrumental resolution time, but varies with the biomolecular structure and the amount of hydration, while the one of water is merely a resolution effect. |
| format | Article |
| id | doaj-art-37d0bfcaa9dc4e92a75f28fccf7b89a6 |
| institution | DOAJ |
| issn | 2050-084X |
| language | English |
| publishDate | 2024-08-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj-art-37d0bfcaa9dc4e92a75f28fccf7b89a62025-08-20T03:06:43ZengeLife Sciences Publications LtdeLife2050-084X2024-08-011310.7554/eLife.95665Decoupling of the onset of anharmonicity between a protein and its surface water around 200 KLirong Zheng0https://orcid.org/0000-0001-6803-5048Bingxin Zhou1https://orcid.org/0000-0002-3897-9766Banghao Wu2Yang Tan3Juan Huang4Madhusudan Tyagi5Victoria García Sakai6Takeshi Yamada7Hugh O'Neill8Qiu Zhang9Liang Hong10https://orcid.org/0000-0003-0107-336XInstitute of Natural Sciences, Shanghai Jiao Tong University, Shanghai, ChinaInstitute of Natural Sciences, Shanghai Jiao Tong University, Shanghai, China; Shanghai National Center for Applied Mathematics (SJTU Center), Shanghai Jiao Tong University, Shanghai, ChinaInstitute of Natural Sciences, Shanghai Jiao Tong University, Shanghai, China; School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, ChinaInstitute of Natural Sciences, Shanghai Jiao Tong University, Shanghai, China; Shanghai National Center for Applied Mathematics (SJTU Center), Shanghai Jiao Tong University, Shanghai, ChinaInstitute of Natural Sciences, Shanghai Jiao Tong University, Shanghai, China; School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, ChinaDepartment of Materials Science and Engineering, University of Maryland, College Park, United States; NIST Center for Neutron Research, National Institute of Standards and Technology (NIST), Gaithersburg, United StatesISIS Pulsed Neutron and Muon Source, Rutherford Appleton Laboratory, Science & Technology Facilities Council, Didcot, United KingdomNeutron Science and Technology Center, Comprehensive Research Organization for Science and Society, Ibaraki, JapanBiology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, United StatesBiology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, United StatesInstitute of Natural Sciences, Shanghai Jiao Tong University, Shanghai, China; Shanghai National Center for Applied Mathematics (SJTU Center), Shanghai Jiao Tong University, Shanghai, China; Zhangjiang Institute for Advanced Study, Shanghai Jiao Tong Univeristy, Shanghai, China; Shanghai Artificial Intelligence Laboratory, Shanghai, ChinaThe protein dynamical transition at ~200 K, where the biomolecule transforms from a harmonic, non-functional form to an anharmonic, functional state, has been thought to be slaved to the thermal activation of dynamics in its surface hydration water. Here, by selectively probing the dynamics of protein and hydration water using elastic neutron scattering and isotopic labeling, we found that the onset of anharmonicity in the two components around 200 K is decoupled. The one in protein is an intrinsic transition, whose characteristic temperature is independent of the instrumental resolution time, but varies with the biomolecular structure and the amount of hydration, while the one of water is merely a resolution effect.https://elifesciences.org/articles/95665decouplingdynamicsproteinwater |
| spellingShingle | Lirong Zheng Bingxin Zhou Banghao Wu Yang Tan Juan Huang Madhusudan Tyagi Victoria García Sakai Takeshi Yamada Hugh O'Neill Qiu Zhang Liang Hong Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K eLife decoupling dynamics protein water |
| title | Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K |
| title_full | Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K |
| title_fullStr | Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K |
| title_full_unstemmed | Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K |
| title_short | Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K |
| title_sort | decoupling of the onset of anharmonicity between a protein and its surface water around 200 k |
| topic | decoupling dynamics protein water |
| url | https://elifesciences.org/articles/95665 |
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