International Journal of Biochemistry, Biophysics & Molecular Biology

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Structural, Conformational and Interactional Investigation of Proteins with Related Sequences and Multiple Structures

Received: 18 April 2018    Accepted: 08 May 2018    Published: 01 June 2018
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Abstract

Homologous proteins are special macromolecules with related primary sequences and multiple native structures and together with sequence-unrelated nonhomologous ones both constitute the protein amazing universe. Here is made a thorough sample selection, and employed quantitative predictions to analyze structures, conformations, steric and hydrophobic interactions and underlying molecular mechanisms in proteins via two coarse-grained (hydrophobic-polar, large-small) models. First, five empirical relations from nonhomologous samples are determined correlating large and hydrophobic residue sequences from primary to helix and β-sheet structures of functional conformations. When applied to homologous proteins, such empirical relations allow precisely surveying the interaction performance, identifying four types of molecular mechanisms, and computing the stability level in conformation ensembles. 1764 structural inspections capture essential features and furnish structural-interactional insights for homologous proteins, as well as suggest a fruitful way for better understanding conformational variability in biomolecular processes such as protein evolution, dynamics, folding and design.

DOI 10.11648/j.ijbbmb.20180302.11
Published in International Journal of Biochemistry, Biophysics & Molecular Biology (Volume 3, Issue 2, June 2018)
Page(s) 19-29
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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

Coarse-Grained Model, Conformational Ensemble, Homologous Protein, Molecular Sequence Data, Structural Homology, Sequence-Structure Alignment

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Author Information
  • Department of Physics and Chemistry, Faculty of Pharmaceutical Sciences of Ribeir?o Preto, University of S?o Paulo, Ribeir?o Preto, S?o Paulo, Brazil

  • Department of Physics and Chemistry, Faculty of Pharmaceutical Sciences of Ribeir?o Preto, University of S?o Paulo, Ribeir?o Preto, S?o Paulo, Brazil

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  • APA Style

    Lessandra Eller, Luiz Rocha. (2018). Structural, Conformational and Interactional Investigation of Proteins with Related Sequences and Multiple Structures. International Journal of Biochemistry, Biophysics & Molecular Biology, 3(2), 19-29. https://doi.org/10.11648/j.ijbbmb.20180302.11

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    ACS Style

    Lessandra Eller; Luiz Rocha. Structural, Conformational and Interactional Investigation of Proteins with Related Sequences and Multiple Structures. Int. J. Biochem. Biophys. Mol. Biol. 2018, 3(2), 19-29. doi: 10.11648/j.ijbbmb.20180302.11

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    AMA Style

    Lessandra Eller, Luiz Rocha. Structural, Conformational and Interactional Investigation of Proteins with Related Sequences and Multiple Structures. Int J Biochem Biophys Mol Biol. 2018;3(2):19-29. doi: 10.11648/j.ijbbmb.20180302.11

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  • @article{10.11648/j.ijbbmb.20180302.11,
      author = {Lessandra Eller and Luiz Rocha},
      title = {Structural, Conformational and Interactional Investigation of Proteins with Related Sequences and Multiple Structures},
      journal = {International Journal of Biochemistry, Biophysics & Molecular Biology},
      volume = {3},
      number = {2},
      pages = {19-29},
      doi = {10.11648/j.ijbbmb.20180302.11},
      url = {https://doi.org/10.11648/j.ijbbmb.20180302.11},
      eprint = {https://download.sciencepg.com/pdf/10.11648.j.ijbbmb.20180302.11},
      abstract = {Homologous proteins are special macromolecules with related primary sequences and multiple native structures and together with sequence-unrelated nonhomologous ones both constitute the protein amazing universe. Here is made a thorough sample selection, and employed quantitative predictions to analyze structures, conformations, steric and hydrophobic interactions and underlying molecular mechanisms in proteins via two coarse-grained (hydrophobic-polar, large-small) models. First, five empirical relations from nonhomologous samples are determined correlating large and hydrophobic residue sequences from primary to helix and β-sheet structures of functional conformations. When applied to homologous proteins, such empirical relations allow precisely surveying the interaction performance, identifying four types of molecular mechanisms, and computing the stability level in conformation ensembles. 1764 structural inspections capture essential features and furnish structural-interactional insights for homologous proteins, as well as suggest a fruitful way for better understanding conformational variability in biomolecular processes such as protein evolution, dynamics, folding and design.},
     year = {2018}
    }
    

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    T1  - Structural, Conformational and Interactional Investigation of Proteins with Related Sequences and Multiple Structures
    AU  - Lessandra Eller
    AU  - Luiz Rocha
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    T2  - International Journal of Biochemistry, Biophysics & Molecular Biology
    JF  - International Journal of Biochemistry, Biophysics & Molecular Biology
    JO  - International Journal of Biochemistry, Biophysics & Molecular Biology
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    AB  - Homologous proteins are special macromolecules with related primary sequences and multiple native structures and together with sequence-unrelated nonhomologous ones both constitute the protein amazing universe. Here is made a thorough sample selection, and employed quantitative predictions to analyze structures, conformations, steric and hydrophobic interactions and underlying molecular mechanisms in proteins via two coarse-grained (hydrophobic-polar, large-small) models. First, five empirical relations from nonhomologous samples are determined correlating large and hydrophobic residue sequences from primary to helix and β-sheet structures of functional conformations. When applied to homologous proteins, such empirical relations allow precisely surveying the interaction performance, identifying four types of molecular mechanisms, and computing the stability level in conformation ensembles. 1764 structural inspections capture essential features and furnish structural-interactional insights for homologous proteins, as well as suggest a fruitful way for better understanding conformational variability in biomolecular processes such as protein evolution, dynamics, folding and design.
    VL  - 3
    IS  - 2
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