Upload resources

Upload your works to SEDICI to increase its visibility and improve its impact

 

Show simple item record

dc.date.accessioned 2019-10-24T17:03:00Z
dc.date.available 2019-10-24T17:03:00Z
dc.date.issued 2012
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/84010
dc.description.abstract The role of fatty acid binding proteins as intracellular fatty acid transporters may require their direct interaction with membranes. In this way different mechanisms have been previously characterized through experimental studies suggesting different models for FABPs-membrane association, although the process in which the molecule adsorbs to the membrane remains to be elucidated. To estimate the importance of the electrostatic energy in the FABP-membrane interaction, we computationally modeled the interaction of different FABPs with both anionic and neutral membranes. Free Electrostatic Energy of Binding (dE), was computed using Finite Difference Poisson Boltzmann Equation (FDPB) method as implemented in APBS (Adaptive Poisson Boltzmann Solver). Based on the computational analysis, it is found that recruitment to membranes is facilitated by non-specific electrostatic interactions. Also energetic analysis can quantitatively differentiate among the mechanisms of membrane association proposed and determinate the most energetically favorable configuration for the membrane-associated states of different FABPs. This type of calculations could provide a starting point for further computational or experimental analysis. en
dc.format.extent 1691-1697 es
dc.language en es
dc.subject Biomolecular modeling es
dc.subject Electrostatic interaction es
dc.subject Fatty acid binding protein es
dc.subject Molecular dynamics simulation es
dc.subject Protein-membrane interaction es
dc.subject Structure-function relation es
dc.title Similar structures but different mechanisms: prediction of FABPs-membrane interaction by electrostatic calculation en
dc.type Articulo es
sedici.identifier.other doi:10.1016/j.bbamem.2012.03.003 es
sedici.identifier.other eid:2-s2.0-84859882326 es
sedici.identifier.issn 0005-2736 es
sedici.creator.person Zamarreño, Fernando es
sedici.creator.person Herrera, Fernando E. es
sedici.creator.person Córsico, Betina es
sedici.creator.person Costabel, Marcelo D. es
sedici.subject.materias Bioquímica es
sedici.description.fulltext true es
mods.originInfo.place Instituto de Investigaciones Bioquímicas de La Plata es
sedici.subtype Articulo es
sedici.rights.license Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
sedici.rights.uri http://creativecommons.org/licenses/by-nc-sa/4.0/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle Biochimica et Biophysica Acta - Biomembranes es
sedici.relation.journalVolumeAndIssue vol. 1818, no. 7 es
sedici.rights.sherpa * Color: verde* Pre-print del autor: si* Post-print del autor: si* Versión de editor/PDF:no* Condiciones:>>Authors pre-print on any website, including arXiv and RePEC>>Author's post-print on author's personal website immediately>>Author's post-print on open access repository after an embargo period of between 12 months and 48 months>>Permitted deposit due to Funding Body, Institutional and Governmental policy or mandate, may be required to comply with embargo periods of 12 months to 48 months>>Author's post-print may be used to update arXiv and RepEC>>La versión de editor/PDF no puede utilizarse>>Debe enlazar a la versión de editor con DOI>>Author's post-print must be released with a Creative Commons Attribution Non-Commercial No Derivatives License>>Publisher last reviewed on 03/06/2015* Link a Sherpa: http://sherpa.ac.uk/romeo/issn/0005-2736/es/


Download Files

This item appears in the following Collection(s)

Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) Except where otherwise noted, this item's license is described as Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)