Abstract
The interaction between protein and water plays a pivotal role in shaping the structure, dynamics, and function of biomacromolecules. A comprehensive understanding of this intricate interplay necessitates a systematic evaluation of interaction strength and its consequential impact on the dynamics of proteins and water across diverse protein systems. Despite numerous works on understanding the dynamics of water and proteins and the coupling between them, there are still unanswered questions. Here, we combine neutron scattering and isotope labeling to probe the dynamics of proteins and their hydration water in a variety of protein systems. We consider proteins of different structures and varying thermostability as well as proteins within living cells with distinct growth temperatures. Simultaneous characterization of protein and hydration water dynamics across diverse systems was achieved. Moreover, we performed water sorption isothermal measurements on three representative proteins to correlate the observed dynamics with the strength of the interaction energies governing each system. The experimental results underscore that proteins manifesting stronger attractive interactions with water display diffusionlike dynamics with higher flexibility upon hydration, concomitant with a reduced mobility in hydration water. Significantly, our findings suggest that, in fact, it is the interaction between protein and its hydration water that facilitates the transfer of mobility from water to protein, with stronger interactions correlating to greater protein flexibility and slower hydration water diffusion.
| Original language | English |
|---|---|
| Article number | 033316 |
| Journal | Physical Review Research |
| Volume | 6 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jul 2024 |
Funding
This paper was supported by the National Natural Science Foundation of China (Grants No. 12204302 and No. 42106087), the Shanghai Pujiang Program (Grant No. 22PJ1406900), the Startup Fund for Young Faculty at SJTU, the Oceanic Interdisciplinary Program of SJTU (Project No. SL2022MS018), the Natural Science Foundation of Shanghai (Grant No. 23ZR1431700), SJTU Scientific and Technological Innovation Funds (21X010200843), the Student Innovation Center at SJTU. H.O. and Q.Z. acknowledge the support of Center for Structural Molecular Biology (FWPERKP291) funded by the U.S. Department of Energy Office of Biological and Environmental Research. The authors are grateful for the support from the Analytical Instrumentation Center (Grant No. SPST-AIC10112914), SPST, ShanghaiTech University. 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-2010792. The neutron experiment at the Materials and Life Science Experimental Facility of the J-PARC was performed under two user programs (Proposals No. 2019A0020 and No. 2022B0182). Experiments at the ISIS Neutron and Muon Source were supported by a beamtime allocation RB1800112 from the Science and Technology Facilities Council. We acknowledge the support of the Australian Centre for Neutron Scattering (ACNS), ANSTO, and the Australian Government through the National Collaborative Research Infrastructure Strategy, in supporting the neutron research infrastructure used in this paper via ACNS Proposal No. P9325. We would like to thank Dr. Na Li from BL19U2 beamline of SSRF for the help with synchrotron SAXS measurements on No. 2022-NFPS-PT-007003.