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

Kholmirzo T. Kholmurodov

doi:doi:10.11648/j.bio.20130101.12

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

Kholmirzo T. Kholmurodov

Published in American Journal of Bioscience and Bioengineering (Volume 1, Issue 1)

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.

Published in	American Journal of Bioscience and Bioengineering (Volume 1, Issue 1)
DOI	10.11648/j.bio.20130101.12
Page(s)	7-16
Creative Commons	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), 2013. Published by Science Publishing Group

Keywords

Molecular Dynamics, Structure Conformation, Proteins, Mutations, Diseases

References

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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://article.sciencepublishinggroup.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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TY  - JOUR
T1  - Molecular Dynamics Study of the Effect of Induced Mutations on the Protein Structures Associated with Diseases of A Radiobiological Nature
AU  - Kholmirzo T. Kholmurodov
Y1  - 2013/02/20
PY  - 2013
N1  - https://doi.org/10.11648/j.bio.20130101.12
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
SP  - 7
EP  - 16
PB  - Science Publishing Group
SN  - 2328-5893
UR  - https://doi.org/10.11648/j.bio.20130101.12
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
IS  - 1
ER  -

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Kholmirzo T. Kholmurodov

Laboratory of Radiation Biology, Joint Institute for Nuclear Research

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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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ACS Style

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://article.sciencepublishinggroup.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}
}

Copy | Download

TY  - JOUR
T1  - Molecular Dynamics Study of the Effect of Induced Mutations on the Protein Structures Associated with Diseases of A Radiobiological Nature
AU  - Kholmirzo T. Kholmurodov
Y1  - 2013/02/20
PY  - 2013
N1  - https://doi.org/10.11648/j.bio.20130101.12
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
SP  - 7
EP  - 16
PB  - Science Publishing Group
SN  - 2328-5893
UR  - https://doi.org/10.11648/j.bio.20130101.12
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
IS  - 1
ER  -

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