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dc.date.accessioned 2019-10-02T14:05:26Z
dc.date.available 2019-10-02T14:05:26Z
dc.date.issued 2010-07
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/82477
dc.description.abstract It has been suggested that above a critical protein concentration, fish Type III antifreeze protein (AFP III) selfassembles to form micelle-like structures that may play a key role In antifreeze activity. To understand the complex activity of AFP III, a comprehensive description of its association state and structural organization in solution is necessary. We used analytical ultracentrifugation, analytical size-exclusion chromatography, and dynamic light scattering to characterize the interactions and homogeneity of AFP III in solution. Small-angle neutron scattering was used to determine the low-resolution structure in solution. Our results clearly show that at concentrations up to 20 mg mL-1 and at temperatures of 20°C, 6°C, and 4°C, AFP III is monomeric in solution and adopts a structure compatible with that determined by crystallography. Surface tension measurements show a propensity of AFP III to localize at the air/water interface, but this surface activity is not correlated with any aggregation in the bulk. These results support the hypothesis that each AFP III molecule acts independently of the others, and that specific intermolecular interactions between monomers are not required for binding to ice. The lack of attractive interactions between monomers may be functionally important, allowing for more efficient binding and covering of the ice surface. en
dc.format.extent 609-618 es
dc.language en es
dc.subject Air es
dc.subject Animals es
dc.subject Antifreeze Proteins, Type III es
dc.subject Chromatography, Gel es
dc.subject Light es
dc.subject Models, Molecular es
dc.subject Molecular Weight es
dc.subject Neutron Diffraction es
dc.subject Scattering, Radiation es
dc.subject Scattering, Small Angle es
dc.subject Solutions es
dc.subject Surface Tension es
dc.subject Ultracentrifugation es
dc.subject Water es
dc.title Structure and interactions of fish type III antifreeze protein in solution en
dc.type Articulo es
sedici.identifier.other https://doi.org/10.1016/j.bpj.2010.04.030 es
sedici.identifier.issn 00063495 es
sedici.creator.person Salvay, Andrés Gerardo es
sedici.creator.person Gabel, Frank es
sedici.creator.person Pucci, Bernard es
sedici.creator.person Santos, Javier es
sedici.creator.person Howards, Eduardo es
sedici.creator.person Ebel, Christine es
sedici.subject.materias Física es
sedici.description.fulltext true 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 Biophysical Journal es
sedici.relation.journalVolumeAndIssue vol. 99, no. 2 es


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Creative Commons Attribution 4.0 International (CC BY 4.0) Excepto donde se diga explícitamente, este item se publica bajo la siguiente licencia Creative Commons Attribution 4.0 International (CC BY 4.0)