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Updated: Aug 23, 2025

Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy

Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy

Published on: August 13, 2019

Detecting the First Hydration Shell Structure around Biomolecules at Interfaces.

Daniel Konstantinovsky^1,2, Ethan A Perets¹, Ty Santiago³

¹Department of Chemistry, Yale University, New Haven, Connecticut 06520, United States.

ACS Central Science

|October 31, 2022

Summary

This summary is machine-generated.

Chiral sum frequency generation (SFG) spectroscopy exclusively probes the first hydration shell around proteins. This technique reveals protein-water interactions at interfaces, advancing biological studies.

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Last Updated: Aug 23, 2025

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In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

Published on: February 15, 2016

Area of Science:

Biophysics
Chemical Physics
Structural Biology

Background:

Studying water's role in biological processes is challenging due to background noise.
Biomolecular hydration at interfaces differs from bulk solution, complicating *in situ* analysis.
Probing the first hydration shell of biomolecules is crucial for understanding biological functions.

Purpose of the Study:

To investigate chirality transfer from proteins to surrounding water molecules using chiral SFG spectroscopy.
To understand the molecular basis of hydration shell selectivity at biological interfaces.
To establish chiral SFG as a tool for studying biomolecular hydration structures.

Main Methods:

Experimental and computational studies utilizing chiral sum frequency generation (SFG) spectroscopy.
Analysis of chirality transfer from protein structures to water molecules.
Investigating protein-water hydrogen-bonding interactions and asymmetry.

Main Results:

Chiral SFG spectroscopy selectively probes the first hydration shell around proteins.
The technique demonstrates high sensitivity to protein structure and specific protein-water interactions.
Evidence of chirality transfer from the protein to the immediate water layer was observed.

Conclusions:

Chiral SFG is a powerful method for studying the structure of the first hydration shell around biomolecules at interfaces.
This technique offers new avenues for exploring biological interfaces and hydration dynamics.
The findings contribute to understanding fundamental biological processes and the molecular origins of life.