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Understanding water: molecular dynamics simulations of myoglobin
W Gu1, A E Garcia, B P Schoenborn
1Los Alamos National Laboratory, New Mexico 87545, USA.
Basic Life Sciences
|January 1, 1996
Summary
Molecular dynamics simulations reveal that most water molecules in carbon monoxide myoglobin are labile, not tightly bound. This highlights water
Area of Science:
- Biophysics
- Computational Biology
- Structural Biology
Background:
- Myoglobin's hydration is crucial for its structure and function.
- Neutron diffraction provides insights into protein-bound water molecules.
Purpose of the Study:
- To evaluate the stability of water molecules bound to carbon monoxide myoglobin using molecular dynamics simulations.
- To compare protein hydration in solution versus crystalline states.
Main Methods:
- Molecular dynamics simulations were performed on a carbon monoxide myoglobin structure obtained from neutron diffraction analysis.
- Simulations analyzed the hydrogen bonding and lability of water molecules.
Main Results:
- Only a small fraction of water molecules are tightly bound to myoglobin atoms.
- Most water molecules exhibit labile behavior, with dynamic hydrogen bond formation and breakage.
- Protein packing in crystals influences solvent structure compared to solution.
Conclusions:
- Water solvent plays a critical role in protein dynamics and structural stability.
- Simulation findings help explain discrepancies observed in experimental studies of protein hydration (NMR, neutron, and X-ray diffraction).
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