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08:23
Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry
Published on: November 5, 2019
Simple model of sickle hemogloblin
Andrey Shiryayev1, Xiaofei Li, J D Gunton
1Department of Physics, Lehigh University, Bethlehem, PA 18015, USA. andrey@lehigh.edu
The Journal of Chemical Physics
|July 20, 2006
Summary
This study simulates sickle hemoglobin interactions using a simplified two-patch model. Monte Carlo simulations reveal transitions from monomers to chains, mimicking sickle cell disease polymerization.
Area of Science:
- Biophysics
- Computational Biology
- Molecular Modeling
Background:
- Sickle hemoglobin (HbS) polymerization is central to sickle cell disease pathogenesis.
- Understanding HbS interactions requires accurate molecular models and simulation parameters.
- Existing models often lack detailed interaction parameters for accurate solutions.
Purpose of the Study:
- To develop a simplified microscopic model for sickle hemoglobin interactions.
- To investigate HbS nucleation mechanisms through computational simulation.
- To explore the transition from monomers to polymeric structures in HbS.
Main Methods:
- Utilized the Protein Data Bank for structural information.
- Performed Monte Carlo simulations on a simplified two-patch model of HbS.
- Analyzed the equation of state for the simulated protein model.
Main Results:
- Observed a transition from monomers to one-dimensional chains with increasing molecular density.
- The simulation results resemble the polymerization of HbS molecules in solution.
- A competition between chain formation and crystallization was identified in the model.
Conclusions:
- The simplified two-patch model provides insights into HbS polymerization.
- Monte Carlo simulations offer a viable approach for studying HbS nucleation.
- Simulation results align with theoretical models for globular protein interactions.
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