Combining THz spectroscopy and MD simulations to study protein-hydration coupling.

Area of Science:

• Physical Chemistry
• Biophysics
• Computational Biology

Background:

• Understanding protein hydration dynamics is crucial for comprehending protein function and folding.
• The influence of protein structure on the dynamic properties of surrounding water remains an active area of research.

Purpose of the Study:

• To investigate the dynamical properties of water in protein solvation shells using THz spectroscopy and MD simulations.
• To determine how protein folding state affects the characteristics of the dynamical solvation shell.
• To elucidate the molecular mechanisms underlying water dynamics retardation near proteins.

Main Methods:

• Combined Terahertz (THz) spectroscopy with Molecular Dynamics (MD) simulations.
• Conducted kinetic THz absorption studies to observe solvation shell formation.
• Utilized MD simulations to reproduce experimental results and gain molecular insights.

Main Results:

• Solvation dynamics are influenced over several hydration layers, exceeding the range of static properties.
• The properties of the dynamical solvation shell are dependent on the protein's folding state.
• Observed the formation of the dynamical solvation shell during protein folding via kinetic THz absorption.

Conclusions:

• Protein folding significantly impacts the extended dynamical solvation shell of water.
• MD simulations successfully replicate experimental findings, supporting a molecular understanding of water dynamics retardation.
• The study provides insights into the interplay between protein structure and water dynamics at the molecular level.