Abstract
In this work, we present a classical molecular dynamical simulation of human neuroglobin (Ngb) proteins with and without mutation at the distal position. Our aim is to investigate the role of the distal residue in the stability of Ngb. The simulation has been performed using Gromacs software with Gromos96 force field. We designed a mutant Ngb by mutating histidine His64 residue to valine residue. The results showed that, the mutant H64V would lead to the less stability in the inner structure of the proteins. Moreover, the mutation strongly affects the properties of the heme group. Obvious changes in the high-order structure of the mutant protein can also be observed.
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Acknowledgements
This work was supported by the Lotus program, Grand No. 45/2012/HD-NDT. We thank S. Bernad and V. Derrien for fruitfully discussion, and A-.T-.V. Nguyen for carefully reading of the manuscript.
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Bui, T.L.Q., Hoang, V.T., Nguyen, TL.H., Ngo, V.T. (2018). Effect of H64V Mutation on the Dynamical Properties of Human Neuroglobin: A Simulation Study. In: Vo Van, T., Nguyen Le, T., Nguyen Duc, T. (eds) 6th International Conference on the Development of Biomedical Engineering in Vietnam (BME6) . BME 2017. IFMBE Proceedings, vol 63. Springer, Singapore. https://doi.org/10.1007/978-981-10-4361-1_47
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DOI: https://doi.org/10.1007/978-981-10-4361-1_47
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