Mostrar el registro sencillo del ítem
dc.contributor.author
Zaccai, Giuseppe
dc.contributor.author
Bagyan, Irina
dc.contributor.author
Combet, Jérôme
dc.contributor.author
Cuello, Gabriel J.
dc.contributor.author
Demé, Bruno
dc.contributor.author
Fichou, Yann
dc.contributor.author
Gallat, François Xavier
dc.contributor.author
Galván Josa, Víctor Martín
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.contributor.author
Von Gronau, Susanne
dc.contributor.author
Haertlein, Michael
dc.contributor.author
Martel, Anne
dc.contributor.author
Moulin, Martine
dc.contributor.author
Neumann, Markus
dc.contributor.author
Weik, Martin
dc.contributor.author
Oesterhelt, Dieter
dc.date.available
2023-01-27T17:48:01Z
dc.date.issued
2016-08
dc.identifier.citation
Zaccai, Giuseppe; Bagyan, Irina; Combet, Jérôme; Cuello, Gabriel J.; Demé, Bruno; et al.; Neutrons describe ectoine effects on water H-bonding and hydration around a soluble protein and a cell membrane; Nature Publishing Group; Scientific Reports; 6; 8-2016; 1-12
dc.identifier.issn
2045-2322
dc.identifier.uri
http://hdl.handle.net/11336/185992
dc.description.abstract
Understanding adaptation to extreme environments remains a challenge of high biotechnological potential for fundamental molecular biology. The cytosol of many microorganisms, isolated from saline environments, reversibly accumulates molar concentrations of the osmolyte ectoine to counterbalance fluctuating external salt concentrations. Although they have been studied extensively by thermodynamic and spectroscopic methods, direct experimental structural data have, so far, been lacking on ectoine-water-protein interactions. In this paper, in vivo deuterium labeling, small angle neutron scattering, neutron membrane diffraction and inelastic scattering are combined with neutron liquids diffraction to characterize the extreme ectoine-containing solvent and its effects on purple membrane of H. salinarum and E. coli maltose binding protein. The data reveal that ectoine is excluded from the hydration layer at the membrane surface and does not affect membrane molecular dynamics, and prove a previous hypothesis that ectoine is excluded from a monolayer of dense hydration water around the soluble protein. Neutron liquids diffraction to atomic resolution shows how ectoine enhances the remarkable properties of H-bonds in water - properties that are essential for the proper organization, stabilization and dynamics of biological structures.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Nature Publishing Group
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
ECTOINE
dc.subject
NEUTRON SCATTERING TECHNQUES
dc.subject
HALOMONAS TITANICAE
dc.subject.classification
Biología Celular, Microbiología
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.subject.classification
Ciencias Biológicas
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.title
Neutrons describe ectoine effects on water H-bonding and hydration around a soluble protein and a cell membrane
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-01-27T16:36:40Z
dc.journal.volume
6
dc.journal.pagination
1-12
dc.journal.pais
Estados Unidos
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.description.fil
Fil: Zaccai, Giuseppe. Institut Laue Langevin; Francia
dc.description.fil
Fil: Bagyan, Irina. No especifíca;
dc.description.fil
Fil: Combet, Jérôme. Institut Laue Langevin; Francia
dc.description.fil
Fil: Cuello, Gabriel J.. Institut Laue Langevin; Francia
dc.description.fil
Fil: Demé, Bruno. Institut Laue Langevin; Francia
dc.description.fil
Fil: Fichou, Yann. No especifíca;
dc.description.fil
Fil: Gallat, François Xavier. No especifíca;
dc.description.fil
Fil: Galván Josa, Víctor Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Física Enrique Gaviola. Universidad Nacional de Córdoba. Instituto de Física Enrique Gaviola; Argentina
dc.description.fil
Fil: Von Gronau, Susanne. Max-planck-institut Für Biochemie; Alemania
dc.description.fil
Fil: Haertlein, Michael. Institut Laue Langevin; Francia
dc.description.fil
Fil: Martel, Anne. Institut Laue Langevin; Francia
dc.description.fil
Fil: Moulin, Martine. Institut Laue Langevin; Francia
dc.description.fil
Fil: Neumann, Markus. No especifíca;
dc.description.fil
Fil: Weik, Martin. No especifíca;
dc.description.fil
Fil: Oesterhelt, Dieter. Max-planck-institut Für Biochemie; Alemania
dc.journal.title
Scientific Reports
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1038/srep31434
Archivos asociados