American Journal of Bioscience and Bioengineering

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Molecular Dynamics Study of the Effect of Induced Mutations on the Protein Structures Associated with Diseases of A Radiobiological Nature

Received: 21 January 2013    Accepted:     Published: 20 February 2013
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Abstract

The induced mutations in biological molecules, such as DNA and proteins, have quite a different nature (envi-ronmental factors, viruses, ionizing radiation, mutagenic chemicals, inherited genetic alterations, etc.). Induced mutations can destroy the existing chemical (hydrogen) bonds in the native molecular structures or, on the contrary, create new chem-ical (hydrogen) bonds that do not normally exist there. In protein structures, the cause of such changes might be the substi-tution of one or several specific amino acid residues (point mutations). At the atomic level, the replacement of one amino acid residue by another causes essential modifications of the molecular force fields of the environment, which can break important hydrogen bonds underlying the structural stability of biological molecules. In this work, based on molecular dy-namics (MD) method, we demonstrate the effect of mutational structure changes on several biological protein models (the p53 oncoprotein, visual pigment rhodopsin, cyclin-dependent kinase, and recA protein). Molecular dynamics simulation is a powerful tool in investigating the structure properties of biological molecules on the atomic and molecular levels, and it has been widely used to study the structural conformational behavior of proteins. We also discuss the scenario of the mutation effects associated with different kinds of diseases that could develop and take place in physiological conditions.

DOI 10.11648/j.bio.20130101.12
Published in American Journal of Bioscience and Bioengineering (Volume 1, Issue 1, February 2013)
Page(s) 7-16
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This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Molecular Dynamics, Structure Conformation, Proteins, Mutations, Diseases

References
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Author Information
  • Laboratory of Radiation Biology, Joint Institute for Nuclear Research; Dubna International University, Dubna, Moscow Region, Russia

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    Kholmirzo T. Kholmurodov. (2013). Molecular Dynamics Study of the Effect of Induced Mutations on the Protein Structures Associated with Diseases of A Radiobiological Nature. American Journal of Bioscience and Bioengineering, 1(1), 7-16. https://doi.org/10.11648/j.bio.20130101.12

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    Kholmirzo T. Kholmurodov. Molecular Dynamics Study of the Effect of Induced Mutations on the Protein Structures Associated with Diseases of A Radiobiological Nature. Am. J. BioSci. Bioeng. 2013, 1(1), 7-16. doi: 10.11648/j.bio.20130101.12

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    Kholmirzo T. Kholmurodov. Molecular Dynamics Study of the Effect of Induced Mutations on the Protein Structures Associated with Diseases of A Radiobiological Nature. Am J BioSci Bioeng. 2013;1(1):7-16. doi: 10.11648/j.bio.20130101.12

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  • @article{10.11648/j.bio.20130101.12,
      author = {Kholmirzo T. Kholmurodov},
      title = {Molecular Dynamics Study of the Effect of Induced Mutations on the Protein Structures Associated with Diseases of A Radiobiological Nature},
      journal = {American Journal of Bioscience and Bioengineering},
      volume = {1},
      number = {1},
      pages = {7-16},
      doi = {10.11648/j.bio.20130101.12},
      url = {https://doi.org/10.11648/j.bio.20130101.12},
      eprint = {https://download.sciencepg.com/pdf/10.11648.j.bio.20130101.12},
      abstract = {The induced mutations in biological molecules, such as DNA and proteins, have quite a different nature (envi-ronmental factors, viruses, ionizing radiation, mutagenic chemicals, inherited genetic alterations, etc.). Induced mutations can destroy the existing chemical (hydrogen) bonds in the native molecular structures or, on the contrary, create new chem-ical (hydrogen) bonds that do not normally exist there. In protein structures, the cause of such changes might be the substi-tution of one or several specific amino acid residues (point mutations). At the atomic level, the replacement of one amino acid residue by another causes essential modifications of the molecular force fields of the environment, which can break important hydrogen bonds underlying the structural stability of biological molecules. In this work, based on molecular dy-namics (MD) method, we demonstrate the effect of mutational structure changes on several biological protein models (the p53 oncoprotein, visual pigment rhodopsin, cyclin-dependent kinase, and recA protein). Molecular dynamics simulation is a powerful tool in investigating the structure properties of biological molecules on the atomic and molecular levels, and it has been widely used to study the structural conformational behavior of proteins. We also discuss the scenario of the mutation effects associated with different kinds of diseases that could develop and take place in physiological conditions.},
     year = {2013}
    }
    

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    T1  - Molecular Dynamics Study of the Effect of Induced Mutations on the Protein Structures Associated with Diseases of A Radiobiological Nature
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    Y1  - 2013/02/20
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    DO  - 10.11648/j.bio.20130101.12
    T2  - American Journal of Bioscience and Bioengineering
    JF  - American Journal of Bioscience and Bioengineering
    JO  - American Journal of Bioscience and Bioengineering
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    AB  - The induced mutations in biological molecules, such as DNA and proteins, have quite a different nature (envi-ronmental factors, viruses, ionizing radiation, mutagenic chemicals, inherited genetic alterations, etc.). Induced mutations can destroy the existing chemical (hydrogen) bonds in the native molecular structures or, on the contrary, create new chem-ical (hydrogen) bonds that do not normally exist there. In protein structures, the cause of such changes might be the substi-tution of one or several specific amino acid residues (point mutations). At the atomic level, the replacement of one amino acid residue by another causes essential modifications of the molecular force fields of the environment, which can break important hydrogen bonds underlying the structural stability of biological molecules. In this work, based on molecular dy-namics (MD) method, we demonstrate the effect of mutational structure changes on several biological protein models (the p53 oncoprotein, visual pigment rhodopsin, cyclin-dependent kinase, and recA protein). Molecular dynamics simulation is a powerful tool in investigating the structure properties of biological molecules on the atomic and molecular levels, and it has been widely used to study the structural conformational behavior of proteins. We also discuss the scenario of the mutation effects associated with different kinds of diseases that could develop and take place in physiological conditions.
    VL  - 1
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