Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K

Lirong Zheng; Bingxin Zhou; Banghao Wu; Yang Tan; Juan Huang; Madhusudan Tyagi; Victoria García Sakai; Takeshi Yamada; Hugh O'neill; Qiu Zhang; Liang Hong

doi:10.7554/eLife.95665

Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K

Lirong Zheng, Bingxin Zhou, Banghao Wu, Yang Tan, Juan Huang, Madhusudan Tyagi, Victoria García Sakai, Takeshi Yamada, Hugh O'neill, Qiu Zhang, Liang Hong

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Article number	RP95665
Journal	eLife
Volume	13
DOIs	https://doi.org/10.7554/eLife.95665
State	Published - 2024

Funding

This work is supported by the National Natural Science Foundation of China (11974239; 62302291), the Innovation Program of Shanghai Municipal Education Commission (2019-01-07-00-02-E00076). HO\u2019N and QZ acknowledge the support of Center for Structural Molecular Biology (FWPERKP291) funded by the U.S. Department of Energy (DOE) Office of Biological and Environmental Research. Funder Grant reference number Author National Natural Science Foundation of China 11974239 Liang Hong National Natural Science Foundation of China 62302291 Bingxin Zhou Innovation Program of Shanghai Municipal Education Commission 2019-01-07-00-02-E00076 Liang Hong Center for Structural Molecular Biology FWPERKP291 Hugh O'Neill Qiu Zhang The funders had no role in study design, data collection, and interpretation, or the decision to submit the work for publication. All the experimental and computational data are shown in main text. Access to the HFBS was provided by the Center for High-Resolution Neutron Scattering, a partnership between the National Institute of Standards and Technology and the National Science Foundation under Agreement No. DMR-1508249. The neutron experiment at the Materials and Life Science Experimental Facility of the J-PARC was performed under a user program (Proposal No. 2019A0020). We thank STFC for access to neutron scattering facilities at RB1800112. The original data are accessible via data cite: https://doi. org/10.5286/ISIS.E.RB1800112. This work is supported by the National Natural Science Foundation of China (11974239; 62302291), the Innovation Program of Shanghai Municipal Education Commission (2019-01-07-00-02-E00076). HO\u2019N and QZ acknowledge the support of Center for Structural Molecular Biology (FWPERKP291) funded by the U.S. Department of Energy (DOE) Office of Biological and Environmental Research.

Funders	Funder number
Biological and Environmental Research
U.S. Department of Energy
National Institute of Standards and Technology
Shanghai Municipal Education Commission	2019-01-07-00-02-E00076
Center for Structural Molecular Biology	FWPERKP291
National Science Foundation	DMR-1508249
National Natural Science Foundation of China	62302291, 11974239

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10.7554/eLife.95665

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title = "Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K",

abstract = "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.",

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AU - Zheng, Lirong

AU - Zhou, Bingxin

AU - Wu, Banghao

AU - Tan, Yang

AU - Huang, Juan

AU - Tyagi, Madhusudan

AU - Sakai, Victoria García

AU - Yamada, Takeshi

AU - O'neill, Hugh

AU - Zhang, Qiu

AU - Hong, Liang

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AB - 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.

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Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K

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