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dc.date.accessioned 2019-12-02T18:42:46Z
dc.date.available 2019-12-02T18:42:46Z
dc.date.issued 2016
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/86519
dc.description.abstract Crystal diffraction data of heart fatty acid binding protein (H-FABP) in complex with oleic acid were measured at room temperature with high-resolution X-ray and neutron protein crystallography (0.98 and 1.90 Å resolution, respectively). These data provided very detailed information about the cluster of water molecules and the bound oleic acid in the H-FABP large internal cavity. The jointly refined X-ray/neutron structure of H-FABP was complemented by a transferred multipolar electron-density distribution using the parameters of the ELMAMII library. The resulting electron density allowed a precise determination of the electrostatic potential in the fatty acid (FA) binding pocket. Bader's quantum theory of atoms in molecules was then used to study interactions involving the internal water molecules, the FA and the protein. This approach showed H···H contacts of the FA with highly conserved hydrophobic residues known to play a role in the stabilization of long-chain FAs in the binding cavity. The determination of water hydrogen (deuterium) positions allowed the analysis of the orientation and electrostatic properties of the water molecules in the very ordered cluster. As a result, a significant alignment of the permanent dipoles of the water molecules with the protein electrostatic field was observed. This can be related to the dielectric properties of hydration layers around proteins, where the shielding of electrostatic interactions depends directly on the rotational degrees of freedom of the water molecules in the interface. en
dc.format.extent 115-126 es
dc.language en es
dc.subject AIM topological properties es
dc.subject fatty acid binding protein es
dc.subject high-resolution room-temperature X-ray crystallography es
dc.subject Neutron protein crystallography es
dc.subject protein hydration layer es
dc.title High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution en
dc.type Articulo es
sedici.identifier.other doi:10.1107/S2052252515024161 es
sedici.identifier.other eid:2-s2.0-84960440601 es
sedici.identifier.issn 2052-2525 es
sedici.creator.person Howard, Eduardo Ignacio es
sedici.creator.person Guillot, B. es
sedici.creator.person Blakeley, M. P. es
sedici.creator.person Haertlein, M. es
sedici.creator.person Moulin, M. es
sedici.creator.person Mitschler, A. es
sedici.creator.person Cousido Siah, A. es
sedici.creator.person Fadel, F. es
sedici.creator.person Valsecchi, W. M. es
sedici.creator.person Tomizaki, T. es
sedici.creator.person Petrova, T. es
sedici.creator.person Claudot, J. es
sedici.creator.person Podjarny, A. es
sedici.subject.materias Ciencias Exactas es
sedici.description.fulltext true es
mods.originInfo.place Facultad de Ciencias Exactas es
mods.originInfo.place Instituto de Física de Líquidos y Sistemas Biológicos es
sedici.subtype Articulo es
sedici.rights.license Creative Commons Attribution 4.0 International (CC BY 4.0)
sedici.rights.uri http://creativecommons.org/licenses/by/4.0/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle IUCrJ es
sedici.relation.journalVolumeAndIssue vol. 3 es
sedici.rights.sherpa * Color: green * Pre-print del autor: can * Post-print del autor: can * Versión de editor/PDF:can * Condiciones: >>On author's personal website, employer's website, employer's repository, or subject-based repository >>Creative Commons Attribution License >>Authors retain copyright >>Published source must be acknowledged >>Must link to publisher version on IUCr server >>Authors' pre-print must acknowledge submission to journal >>Publisher's version/PDF may be used (authorised electronic re-print) (preferred) >>Publisher's version/PDF (authorised electronic re-print) on PubMed Central and related servers >>All titles are open access journals >>Publisher last contacted on 23/04/2014 * Link a Sherpa: http://sherpa.ac.uk/romeo/issn/2052-2525/es/


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