Web of Science: 3 cites, Scopus: 5 cites, Google Scholar: cites
A protein self-assembly model guided by electrostatic and hydrophobic dipole moments
Mozo-Villarias, Angel (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Querol Murillo, Enrique (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")

Data: 2019
Resum: 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.
Ajuts: Ministerio de Economía y Competitividad BIO2017-84166R
Ministerio de Economía y Competitividad BIO2013-50176-EXP
Drets: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original. Creative Commons
Llengua: Anglès
Document: Article ; recerca ; Versió publicada
Matèria: Capsid ; Computer Simulation ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Protein Subunits ; Proteins ; Rotation ; Static Electricity ; Tobacco Mosaic Virus
Publicat a: PloS one, Vol. 14, issue 4 (April 2019) , art. e0216253, ISSN 1932-6203

DOI: 10.1371/journal.pone.0216253
PMID: 31034513


19 p, 2.2 MB

El registre apareix a les col·leccions:
Documents de recerca > Documents dels grups de recerca de la UAB > Centres i grups de recerca (producció científica) > Ciències de la salut i biociències > Institut de Biotecnologia i de Biomedicina (IBB)
Articles > Articles de recerca
Articles > Articles publicats

 Registre creat el 2020-06-03, darrera modificació el 2022-03-27



   Favorit i Compartir