Decoupling of the Onset of Anharmonicity between a Protein and Its Surface Water around 200 K-Reference-Cited by-同舟云学术

Decoupling of the Onset of Anharmonicity between a Protein and Its Surface Water around 200 K

Published:2024-07-12 Issue: Volume: Page:
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Author:

Zheng Lirong¹²,Zhou Bingxin¹,Wu Banghao¹³,Tan Yang¹,Huang Juan³,Tyagi Madhusudan⁴,Sakai Victoria García⁵,Yamada Takeshi⁶,O’Neill Hugh⁷,Zhang Qiu⁷,Hong Liang¹

Affiliation:

1. Institute of Natural Sciences, Shanghai Jiao Tong University

2. Department of Cell and Developmental Biology & Michigan Neuroscience Institute, University of Michigan Medical School

3. School of Life Sciences and Biotechnology, Shanghai Jiao Tong University

4. NIST Center for Neutron Research, National Institute of Standards and Technology (NIST), Gaithersburg, Maryland 20899, USA & Department of Materials Science and Engineering, University of Maryland

5. ISIS Pulsed Neutron and Muon Source, Rutherford Appleton Laboratory, Science & Technology Facilities Council

6. Neutron Science and Technology Center, Comprehensive Research Organization for Science and Society

7. Biology and Soft Matter Division, Oak Ridge National Laboratory

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 labelling, we found that the onset of anharmonicity in the two components around 200 K are 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.

Publisher

eLife Sciences Publications, Ltd

Link

https://elifesciences.org/reviewed-preprints/95665v2/pdf

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