ArticleJACS Au2025
Visualize Transient Water-Mediated Hydrogen Bonds Facilitating the Formation of Enzymatic Near-Attack Conformers.
Wenqing Xia, Jiawen Chen, Ling Jiang, Meng Lu, Maili Liu, Minghui Yang, Conggang Li, Yixiang Liu
Abstract read
In one paragraphArticle in JACS Au, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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5 · Who and what moneyAuthors and funding
8 authors.
Wenqing XiaState Key Laboratory of Magnetic Resonance Spectroscopy and Imaging, National Center for Magnetic Resonance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430074, China.
Jiawen ChenState Key Laboratory of Magnetic Resonance Spectroscopy and Imaging, National Center for Magnetic Resonance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430074, China.
Ling JiangState Key Laboratory of Magnetic Resonance Spectroscopy and Imaging, National Center for Magnetic Resonance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430074, China.ORCID https://orcid.org/0000-0002-8505-8679 Meng LuState Key Laboratory of Magnetic Resonance Spectroscopy and Imaging, National Center for Magnetic Resonance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430074, China.
Maili LiuState Key Laboratory of Magnetic Resonance Spectroscopy and Imaging, National Center for Magnetic Resonance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430074, China.ORCID https://orcid.org/0000-0002-9359-915X Minghui YangState Key Laboratory of Magnetic Resonance Spectroscopy and Imaging, National Center for Magnetic Resonance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430074, China.
Conggang LiState Key Laboratory of Magnetic Resonance Spectroscopy and Imaging, National Center for Magnetic Resonance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430074, China.ORCID https://orcid.org/0000-0002-5798-1722 Yixiang LiuState Key Laboratory of Magnetic Resonance Spectroscopy and Imaging, National Center for Magnetic Resonance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430074, China.ORCID https://orcid.org/0000-0003-2977-1741 Funding
No grant is acknowledged in the PubMed record.
6 · The paper itselfAbstract
Water-mediated hydrogen bonds are vital to various macromolecular activities, particularly in enzymatic reactions. However, the dynamic nature of these bonds poses challenges for their detection. Currently, there is a lack of methods for directly resolving residues within proteins that form hydrogen bonds with water at the atomic level. Herein, we combined supercooling techniques with an NMR method based on spin transverse relaxation perturbation through rational manipulations of dipolar interactions and quantum coherence to characterize transient water-mediated hydrogen bonds in proteins. After thorough validation on different proteins, we applied this method to the catalysis of adenylate kinase (AdK) from
Indexed as
enzymatic catalysisnear-attack conformationNMRsupercoolingwater-mediated hydrogen bond
Identifiers
PMID41311930
PMCPMC12648308
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