Electro-optical properties characterization of fish type III antifreeze protein

Autores
Salvay, Andrés Gerardo; Santos, Javier; Howard, Eduardo Ignacio
Año de publicación
2007
Idioma
español castellano
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Antifreeze proteins (AFPs) are ice-binding proteins that depress the freezing point of water in a non-colligative manner without a significant modification of the melting point. Found in the blood and tissues of some organisms (such as fish, insects, plants, and soil bacteria), AFPs play an important role in subzero temperature survival. Fish Type III AFP is present in members of the subclass Zoarcoidei. AFPIII are small 7-kDa—or 14-kDa tandem—globular proteins. In the present work, we study the behavior of several physical properties, such as the low-frequency dielectric permittivity spectrum, circular dichroism, and electrical conductivity of Fish Type III AFP solutions measured at different concentrations. The combination of the information obtained from these measurements could be explained through the formation of AFP molecular aggregates or, alternatively, by the existence of some other type of interparticle interactions. Thermal stability and electrooptical behavior, when proteins are dissolved in deuterated water, were also investigated.
Instituto de Física de Líquidos y Sistemas Biológicos
Materia
Física
Antifreeze proteins
AFPIII
Electro-optical behavior
Thermal stability
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/107113
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/107113
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Electro-optical properties characterization of fish type III antifreeze proteinSalvay, Andrés GerardoSantos, JavierHoward, Eduardo IgnacioFísicaAntifreeze proteinsAFPIIIElectro-optical behaviorThermal stabilityAntifreeze proteins (AFPs) are ice-binding proteins that depress the freezing point of water in a non-colligative manner without a significant modification of the melting point. Found in the blood and tissues of some organisms (such as fish, insects, plants, and soil bacteria), AFPs play an important role in subzero temperature survival. Fish Type III AFP is present in members of the subclass Zoarcoidei. AFPIII are small 7-kDa—or 14-kDa tandem—globular proteins. In the present work, we study the behavior of several physical properties, such as the low-frequency dielectric permittivity spectrum, circular dichroism, and electrical conductivity of Fish Type III AFP solutions measured at different concentrations. The combination of the information obtained from these measurements could be explained through the formation of AFP molecular aggregates or, alternatively, by the existence of some other type of interparticle interactions. Thermal stability and electrooptical behavior, when proteins are dissolved in deuterated water, were also investigated.Instituto de Física de Líquidos y Sistemas Biológicos2007info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf389-397http://sedici.unlp.edu.ar/handle/10915/107113spainfo:eu-repo/semantics/altIdentifier/url/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC2565770&blobtype=pdfinfo:eu-repo/semantics/altIdentifier/issn/1573-0689info:eu-repo/semantics/altIdentifier/pmid/19669526info:eu-repo/semantics/altIdentifier/doi/10.1007/s10867-008-9080-5info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-17T10:06:39Zoai:sedici.unlp.edu.ar:10915/107113Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-17 10:06:39.6SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Electro-optical properties characterization of fish type III antifreeze protein
title Electro-optical properties characterization of fish type III antifreeze protein
spellingShingle Electro-optical properties characterization of fish type III antifreeze protein
Salvay, Andrés Gerardo
Física
Antifreeze proteins
AFPIII
Electro-optical behavior
Thermal stability
title_short Electro-optical properties characterization of fish type III antifreeze protein
title_full Electro-optical properties characterization of fish type III antifreeze protein
title_fullStr Electro-optical properties characterization of fish type III antifreeze protein
title_full_unstemmed Electro-optical properties characterization of fish type III antifreeze protein
title_sort Electro-optical properties characterization of fish type III antifreeze protein
dc.creator.none.fl_str_mv Salvay, Andrés Gerardo
Santos, Javier
Howard, Eduardo Ignacio
author Salvay, Andrés Gerardo
author_facet Salvay, Andrés Gerardo
Santos, Javier
Howard, Eduardo Ignacio
author_role author
author2 Santos, Javier
Howard, Eduardo Ignacio
author2_role author
author
dc.subject.none.fl_str_mv Física
Antifreeze proteins
AFPIII
Electro-optical behavior
Thermal stability
topic Física
Antifreeze proteins
AFPIII
Electro-optical behavior
Thermal stability
dc.description.none.fl_txt_mv Antifreeze proteins (AFPs) are ice-binding proteins that depress the freezing point of water in a non-colligative manner without a significant modification of the melting point. Found in the blood and tissues of some organisms (such as fish, insects, plants, and soil bacteria), AFPs play an important role in subzero temperature survival. Fish Type III AFP is present in members of the subclass Zoarcoidei. AFPIII are small 7-kDa—or 14-kDa tandem—globular proteins. In the present work, we study the behavior of several physical properties, such as the low-frequency dielectric permittivity spectrum, circular dichroism, and electrical conductivity of Fish Type III AFP solutions measured at different concentrations. The combination of the information obtained from these measurements could be explained through the formation of AFP molecular aggregates or, alternatively, by the existence of some other type of interparticle interactions. Thermal stability and electrooptical behavior, when proteins are dissolved in deuterated water, were also investigated.
Instituto de Física de Líquidos y Sistemas Biológicos
description Antifreeze proteins (AFPs) are ice-binding proteins that depress the freezing point of water in a non-colligative manner without a significant modification of the melting point. Found in the blood and tissues of some organisms (such as fish, insects, plants, and soil bacteria), AFPs play an important role in subzero temperature survival. Fish Type III AFP is present in members of the subclass Zoarcoidei. AFPIII are small 7-kDa—or 14-kDa tandem—globular proteins. In the present work, we study the behavior of several physical properties, such as the low-frequency dielectric permittivity spectrum, circular dichroism, and electrical conductivity of Fish Type III AFP solutions measured at different concentrations. The combination of the information obtained from these measurements could be explained through the formation of AFP molecular aggregates or, alternatively, by the existence of some other type of interparticle interactions. Thermal stability and electrooptical behavior, when proteins are dissolved in deuterated water, were also investigated.
publishDate 2007
dc.date.none.fl_str_mv 2007
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/107113
url http://sedici.unlp.edu.ar/handle/10915/107113
dc.language.none.fl_str_mv spa
language spa
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC2565770&blobtype=pdf
info:eu-repo/semantics/altIdentifier/issn/1573-0689
info:eu-repo/semantics/altIdentifier/pmid/19669526
info:eu-repo/semantics/altIdentifier/doi/10.1007/s10867-008-9080-5
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
389-397
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.001348

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