A protein self-assembly model guided by electrostatic and hydrophobic dipole moments.
Protein self-assembling is studied under the light of the Biological Membrane model. To this purpose we define a simplified formulation of hydrophobic interaction energy in analogy with electrostatic energy stored in an electric dipole. Self-assembly is considered to be the result of the balanced in...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2019-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0216253 |
| _version_ | 1818935161314607104 |
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| author | Angel Mozo-Villarías Enrique Querol |
| author_facet | Angel Mozo-Villarías Enrique Querol |
| author_sort | Angel Mozo-Villarías |
| collection | DOAJ |
| description | Protein self-assembling is studied under the light of the Biological Membrane model. To this purpose we define a simplified formulation of hydrophobic interaction energy in analogy with electrostatic energy stored in an electric dipole. Self-assembly is considered to be the result of the balanced influence of electrostatic and hydrophobic interactions, limited by steric hindrance as a consequence of the relative proximity of their components. Our analysis predicts the type of interaction that drives an assembly. We study the growth of both electrostatic and hydrophobic energies stored by a protein system as it self-assembles. Each type of assembly is studied by using two examples, PDBid 2OM3 (hydrophobic) and PDBid 3ZEE (electrostatic). Other systems are presented to show the application of our procedure. We also study the relative orientation of the monomers constituting the first dimer of a protein assembly to check whether their relative position provides the optimal interaction energy (energy minimum). It is shown that the inherent orientation of the dimers corresponds to the optimum energy (energy minimum) of assembly compatible with steric limitations. These results confirm and refine our Biological Membrane model of protein self-assembly valid for all open and closed systems. |
| first_indexed | 2024-12-20T05:15:46Z |
| format | Article |
| id | doaj.art-ef23552b173c4b00b7a94132bc813aa9 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-20T05:15:46Z |
| publishDate | 2019-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-ef23552b173c4b00b7a94132bc813aa92022-12-21T19:52:09ZengPublic Library of Science (PLoS)PLoS ONE1932-62032019-01-01144e021625310.1371/journal.pone.0216253A protein self-assembly model guided by electrostatic and hydrophobic dipole moments.Angel Mozo-VillaríasEnrique QuerolProtein self-assembling is studied under the light of the Biological Membrane model. To this purpose we define a simplified formulation of hydrophobic interaction energy in analogy with electrostatic energy stored in an electric dipole. Self-assembly is considered to be the result of the balanced influence of electrostatic and hydrophobic interactions, limited by steric hindrance as a consequence of the relative proximity of their components. Our analysis predicts the type of interaction that drives an assembly. We study the growth of both electrostatic and hydrophobic energies stored by a protein system as it self-assembles. Each type of assembly is studied by using two examples, PDBid 2OM3 (hydrophobic) and PDBid 3ZEE (electrostatic). Other systems are presented to show the application of our procedure. We also study the relative orientation of the monomers constituting the first dimer of a protein assembly to check whether their relative position provides the optimal interaction energy (energy minimum). It is shown that the inherent orientation of the dimers corresponds to the optimum energy (energy minimum) of assembly compatible with steric limitations. These results confirm and refine our Biological Membrane model of protein self-assembly valid for all open and closed systems.https://doi.org/10.1371/journal.pone.0216253 |
| spellingShingle | Angel Mozo-Villarías Enrique Querol A protein self-assembly model guided by electrostatic and hydrophobic dipole moments. PLoS ONE |
| title | A protein self-assembly model guided by electrostatic and hydrophobic dipole moments. |
| title_full | A protein self-assembly model guided by electrostatic and hydrophobic dipole moments. |
| title_fullStr | A protein self-assembly model guided by electrostatic and hydrophobic dipole moments. |
| title_full_unstemmed | A protein self-assembly model guided by electrostatic and hydrophobic dipole moments. |
| title_short | A protein self-assembly model guided by electrostatic and hydrophobic dipole moments. |
| title_sort | protein self assembly model guided by electrostatic and hydrophobic dipole moments |
| url | https://doi.org/10.1371/journal.pone.0216253 |
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