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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
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Entropy connects water structure and dynamics in protein hydration layer
Jayangika N Dahanayake1, Katie R Mitchell-Koch
1Wichita State University, Department of Chemistry, Wichita, Kansas, USA. katie.mitchell-koch@wichita.edu.
Physical Chemistry Chemical Physics : PCCP
|May 22, 2018
Summary
The study reveals that enzyme hydration layers exhibit varied water dynamics linked to surface structure. Denser regions show faster water movement, analogous to bulk water, following the Rosenfeld relationship.
Area of Science:
- Biophysics
- Computational Biology
- Enzymology
Background:
- Understanding protein hydration layers is crucial for enzyme function.
- Water dynamics near protein surfaces differ from bulk water.
- The relationship between hydration structure and dynamics is complex.
Purpose of the Study:
- To investigate the structure and dynamics of water molecules in the hydration layer of Candida Antarctica lipase B (CALB).
- To explore the connections between hydration layer dynamics, solvation shell structure, and protein surface characteristics.
- To determine if the Rosenfeld scaling relationship applies to enzyme hydration layers.
Main Methods:
- Characterization of water molecule structure and dynamics on the CALB surface.
- Division of the CALB surface into regions based on secondary structures (α-helix, β-sheet, loop).
- Multiregression analysis to evaluate the effects of protein surface topology and hydrophobicity.
- Calculation of pairwise entropies from regional radial distribution functions.
Main Results:
- Heterogeneous hydration dynamics were observed across the CALB surface.
- Regions with higher water density exhibited faster dynamics.
- Protein surface topology had a significant effect on hydration layer structure-dynamics.
- Concave and hydrophobic surfaces promoted less dense, more tetrahedral, ice-like water structures with slower dynamics.
- Pairwise entropies scaled logarithmically with local hydration dynamics, supporting the Rosenfeld relationship.
Conclusions:
- The Rosenfeld relationship accurately describes the heterogeneous structure-dynamics of the CALB hydration layer.
- Enzyme surface topology and hydrophobicity significantly influence local water structure and dynamics.
- These findings suggest a potential general principle for biomolecular solvation structure-dynamics.
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