Dynamic entity formed by protein and its hydration water

• Published in: Physical review research Vol. 6; no. 3; p. 033316
• Main Authors: Ye, Yongfeng, Chen, Xiaoxia, Huang, Juan, Zheng, Lirong, Tang, Qingxue, Long, Liuliu, Yamada, Takeshi, Tyagi, Madhusudan, Sakai, Victoria García, O’Neill, Hugh, Zhang, Qiu, de Souza, Nicolas R., Xiao, Xiang, Zhao, Weishu, Hong, Liang, Liu, Zhuo
• Format: Journal Article
• Language: English
• Published: United States American Physical Society 19.09.2024
• ISSN: 2643-1564; 2643-1564
• DOI: 10.1103/PhysRevResearch.6.033316

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. Published by the American Physical Society 2024