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Coupling between lysozyme and trehalose dynamics: microscopic insights from molecular-dynamics simulations.
Taner E Dirama1, Joseph E Curtis, Gustavo A Carri
1Department of Polymer Science, The University of Akron, Akron, Ohio 44325-3909, USA.
The Journal of Chemical Physics
|January 28, 2006
Summary
Molecular dynamics simulations reveal strong dynamical coupling between lysozyme protein and trehalose biopreservative. This protein-trehalose interaction, driven by hydrogen bonds, influences protein relaxation and reveals unique solvent dynamics near the protein surface.
Area of Science:
- Biophysics
- Computational Biology
- Materials Science
Background:
- Trehalose is a biopreservative known for its stabilizing effects on proteins.
- Understanding protein-solvent interactions is crucial for biopreservation and drug delivery.
Purpose of the Study:
- To investigate the dynamical coupling between lysozyme protein and trehalose.
- To elucidate the microscopic origins of protein-solvent interactions and their impact on dynamics.
Main Methods:
- All-atom molecular-dynamics simulations were performed on flexible lysozyme models in trehalose.
- Simulations covered a range of temperatures to observe dynamical changes.
Main Results:
- A strong dynamical coupling between lysozyme and trehalose was observed across temperatures.
- Protein-trehalose coupling originates from interfacial hydrogen bonds, influencing protein structural relaxation.
- Protein dynamics are heterogeneous, with surface atoms showing greater sensitivity to solvent dynamics.
- Trehalose dynamics near the protein surface exhibit enhanced mobility compared to the bulk.
Conclusions:
- Hydrogen bonding is key to protein-trehalose dynamical coupling and protein structural relaxation.
- Heterogeneous protein dynamics and enhanced solvent mobility near the protein surface are significant findings.
- The study provides microscopic insights into dynamical coupling in protein-solvent systems.