气候变化领域集成服务门户(CCPortal): Mirror-image antiparallel β-sheets organize water molecules into superstructures of opposite chirality

CCPortal

DOI	10.1073/PNAS.2015567117
	Mirror-image antiparallel β-sheets organize water molecules into superstructures of opposite chirality
	Perets E.A.; Konstantinovsky D.; Fu L.; Chen J.; Wang H.-F.; Hammes-Schiffer S.; Yan E.C.Y.
发表日期	2021
ISSN	00278424
起始页码	32902
结束页码	32909
卷号	117 期号:52
英文摘要	Biomolecular hydration is fundamental to biological functions. Using phase-resolved chiral sum-frequency generation spectroscopy (SFG), we probe molecular architectures and interactions of water molecules around a self-assembling antiparallel β-sheet protein. We find that the phase of the chiroptical response from the O-H stretching vibrational modes of water flips with the absolute chirality of the (L-) or (D-) antiparallel β-sheet. Therefore, we can conclude that the (D-) antiparallel β-sheet organizes water solvent into a chiral supermolecular structure with opposite handedness relative to that of the (L-) antiparallel β-sheet. We use molecular dynamics to characterize the chiral water superstructure at atomic resolution. The results show that the macroscopic chirality of antiparallel β-sheets breaks the symmetry of assemblies of surrounding water molecules. We also calculate the chiral SFG response of water surrounding (L-) and (D-) LK7β to confirm the presence of chiral water structures. Our results offer a different perspective as well as introduce experimental and computational methodologies for elucidating hydration of biomacromolecules. The findings imply potentially important but largely unexplored roles of water solvent in chiral selectivity of biomolecular interactions and the molecular origins of homochirality in the biological world. © 2020 National Academy of Sciences. All rights reserved.
英文关键词	Chiral SFG; Hydration; Interfaces; Protein; Water
语种	英语
scopus关键词	leucine; lysine; oligopeptide; water; beta sheet; chemical phenomena; chemistry; isomerism; molecular dynamics; protein folding; protein multimerization; Hydrophobic and Hydrophilic Interactions; Isomerism; Leucine; Lysine; Molecular Dynamics Simulation; Oligopeptides; Protein Conformation, beta-Strand; Protein Folding; Protein Multimerization; Water
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/179650
作者单位	Department of Chemistry, Yale University, New Haven, CT 06520, United States; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, United States; Faculty of Materials Science and Engineering, South China University of Technology, Guangzhou, 510640, China; Department of Chemistry, Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Fudan University, Shanghai, 200433, China; School of Science, Westlake University, Hangzhou, 310024, China; Takeda Pharmaceuticals, Cambridge, MA 02139, United States
推荐引用方式 GB/T 7714	Perets E.A.,Konstantinovsky D.,Fu L.,et al. Mirror-image antiparallel β-sheets organize water molecules into superstructures of opposite chirality[J],2021,117(52).
APA	Perets E.A..,Konstantinovsky D..,Fu L..,Chen J..,Wang H.-F..,...&Yan E.C.Y..(2021).Mirror-image antiparallel β-sheets organize water molecules into superstructures of opposite chirality.Proceedings of the National Academy of Sciences of the United States of America,117(52).
MLA	Perets E.A.,et al."Mirror-image antiparallel β-sheets organize water molecules into superstructures of opposite chirality".Proceedings of the National Academy of Sciences of the United States of America 117.52(2021).