Detecting the First Hydration Shell Structure around Biomolecules at Interfaces

Daniel Konstantinovsky, Ethan A. Perets, Ty Santiago, Luis Velarde, Sharon Hammes-Schiffer, Elsa C.Y. Yan

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1404-1414
Number of pages11
JournalACS Central Science
Volume8
Issue number10
DOIs
StatePublished - Oct 26 2022
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • General Chemical Engineering

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