Journal
ACS CENTRAL SCIENCE
Volume 8, Issue 10, Pages 1404-1414Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscentsci.2c00702
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Funding
- National Institutes of Health [National Institutes of Health]
- NSF [CHE-2108690, 5T32GM008283-31]
- NIH [CHE-1753207, 5T32GM008283-32]
- John C. Tully Chemistry Research Fellowship
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Understanding the role of water in biological processes is a central challenge in the life sciences, and chiral SFG spectroscopy can be used to investigate hydration shell structures around proteins, providing new possibilities to address grand research challenges in biology.
Understanding the role of water in biological processes remains a central challenge in the life sciences. Water structures in hydration shells of biomolecules are difficult to study in situ due to overwhelming background from aqueous environments. Biological interfaces introduce additional complexity because biomolecular hydration differs at interfaces compared to bulk solution. Here, we perform experimental and computational studies of chiral sum frequency generation (chiral SFG) spectroscopy to probe chirality transfer from a protein to the surrounding water molecules. This work reveals that chiral SFG probes the first hydration shell around the protein almost exclusively. We explain the selectivity to the first hydration shell in terms of the asymmetry induced by the protein structure and specific protein-water hydrogen-bonding interactions. This work establishes chiral SFG as a powerful technique for studying hydration shell structures around biomolecules at interfaces, presenting new possibilities to address grand research challenges in biology, including the molecular origins of life.
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