期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 117, 期 52, 页码 32902-32909出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2015567117
关键词
chiral SFG; hydration; water; protein; interfaces
资金
- NIH [5T32GM008283-31, 5T32GM008283-32, GM056207]
- NSF [CHE 1905169]
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 beta-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 beta-sheet. Therefore, we can conclude that the (D-) antiparallel beta-sheet organizes water solvent into a chiral supermolecular structure with opposite handedness relative to that of the (L-) antiparallel beta-sheet. We use molecular dynamics to characterize the chiral water superstructure at atomic resolution. The results show that the macroscopic chirality of antiparallel beta-sheets breaks the symmetry of assemblies of surrounding water molecules. We also calculate the chiral SFG response of water surrounding (L-) and (D-) LK7 beta 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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据