Thermodynamic model for the analysis of calorimetric data of oligomeric proteins

Autores
Burgos, Martha Ines; Dassie, Sergio Alberto; Fidelio, Gerardo Daniel
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The thermodynamic parameters for the process of protein unfolding can be obtained through differential scanning calorimetry. However, the unfolding process may not be a two-state one. Between the native and the unfolded state, there may be association or dissociation processes or the formation of an intermediate state. As a consequence of this, the precise interpretation of the calorimetric data should be done with a specific thermodynamic model. In this work, we present two general models for the unfolding process of an oligomeric protein: Nn ⇌ nN ⇌ nD (model A) and Nn ⇌ In ⇌ nD (model B). In model A, the first step represents the dissociation of the oligomer into the monomeric native species, and the second step represents the denaturation process. In model B, the first step represents the conformational change of the oligomer, and the second step represents the dissociation of this species with the concomitant unfolding process. A canonical ensemble was employed to describe these systems, by considering that the total protein concentration remains constant. In the present work, we show and analyze the behavior of these systems in different conditions and how this analysis could help with the identification of the unfolding mechanism experimentally observed.
Fil: Burgos, Martha Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: Dassie, Sergio Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
Fil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Materia
Thermodynamic Model
Ologimeric Proteins
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/76936
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Thermodynamic model for the analysis of calorimetric data of oligomeric proteinsBurgos, Martha InesDassie, Sergio AlbertoFidelio, Gerardo DanielThermodynamic ModelOlogimeric Proteinshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The thermodynamic parameters for the process of protein unfolding can be obtained through differential scanning calorimetry. However, the unfolding process may not be a two-state one. Between the native and the unfolded state, there may be association or dissociation processes or the formation of an intermediate state. As a consequence of this, the precise interpretation of the calorimetric data should be done with a specific thermodynamic model. In this work, we present two general models for the unfolding process of an oligomeric protein: Nn ⇌ nN ⇌ nD (model A) and Nn ⇌ In ⇌ nD (model B). In model A, the first step represents the dissociation of the oligomer into the monomeric native species, and the second step represents the denaturation process. In model B, the first step represents the conformational change of the oligomer, and the second step represents the dissociation of this species with the concomitant unfolding process. A canonical ensemble was employed to describe these systems, by considering that the total protein concentration remains constant. In the present work, we show and analyze the behavior of these systems in different conditions and how this analysis could help with the identification of the unfolding mechanism experimentally observed.Fil: Burgos, Martha Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; ArgentinaFil: Dassie, Sergio Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; ArgentinaFil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaAmerican Chemical Society2008-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/76936Burgos, Martha Ines; Dassie, Sergio Alberto; Fidelio, Gerardo Daniel; Thermodynamic model for the analysis of calorimetric data of oligomeric proteins; American Chemical Society; Journal of Physical Chemistry B; 112; 45; 12-2008; 14325-143331520-61061089-5647CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/18939789info:eu-repo/semantics/altIdentifier/doi/10.1021/jp804465cinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:36:38Zoai:ri.conicet.gov.ar:11336/76936instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:36:38.708CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Thermodynamic model for the analysis of calorimetric data of oligomeric proteins
title Thermodynamic model for the analysis of calorimetric data of oligomeric proteins
spellingShingle Thermodynamic model for the analysis of calorimetric data of oligomeric proteins
Burgos, Martha Ines
Thermodynamic Model
Ologimeric Proteins
title_short Thermodynamic model for the analysis of calorimetric data of oligomeric proteins
title_full Thermodynamic model for the analysis of calorimetric data of oligomeric proteins
title_fullStr Thermodynamic model for the analysis of calorimetric data of oligomeric proteins
title_full_unstemmed Thermodynamic model for the analysis of calorimetric data of oligomeric proteins
title_sort Thermodynamic model for the analysis of calorimetric data of oligomeric proteins
dc.creator.none.fl_str_mv Burgos, Martha Ines
Dassie, Sergio Alberto
Fidelio, Gerardo Daniel
author Burgos, Martha Ines
author_facet Burgos, Martha Ines
Dassie, Sergio Alberto
Fidelio, Gerardo Daniel
author_role author
author2 Dassie, Sergio Alberto
Fidelio, Gerardo Daniel
author2_role author
author
dc.subject.none.fl_str_mv Thermodynamic Model
Ologimeric Proteins
topic Thermodynamic Model
Ologimeric Proteins
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The thermodynamic parameters for the process of protein unfolding can be obtained through differential scanning calorimetry. However, the unfolding process may not be a two-state one. Between the native and the unfolded state, there may be association or dissociation processes or the formation of an intermediate state. As a consequence of this, the precise interpretation of the calorimetric data should be done with a specific thermodynamic model. In this work, we present two general models for the unfolding process of an oligomeric protein: Nn ⇌ nN ⇌ nD (model A) and Nn ⇌ In ⇌ nD (model B). In model A, the first step represents the dissociation of the oligomer into the monomeric native species, and the second step represents the denaturation process. In model B, the first step represents the conformational change of the oligomer, and the second step represents the dissociation of this species with the concomitant unfolding process. A canonical ensemble was employed to describe these systems, by considering that the total protein concentration remains constant. In the present work, we show and analyze the behavior of these systems in different conditions and how this analysis could help with the identification of the unfolding mechanism experimentally observed.
Fil: Burgos, Martha Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: Dassie, Sergio Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
Fil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
description The thermodynamic parameters for the process of protein unfolding can be obtained through differential scanning calorimetry. However, the unfolding process may not be a two-state one. Between the native and the unfolded state, there may be association or dissociation processes or the formation of an intermediate state. As a consequence of this, the precise interpretation of the calorimetric data should be done with a specific thermodynamic model. In this work, we present two general models for the unfolding process of an oligomeric protein: Nn ⇌ nN ⇌ nD (model A) and Nn ⇌ In ⇌ nD (model B). In model A, the first step represents the dissociation of the oligomer into the monomeric native species, and the second step represents the denaturation process. In model B, the first step represents the conformational change of the oligomer, and the second step represents the dissociation of this species with the concomitant unfolding process. A canonical ensemble was employed to describe these systems, by considering that the total protein concentration remains constant. In the present work, we show and analyze the behavior of these systems in different conditions and how this analysis could help with the identification of the unfolding mechanism experimentally observed.
publishDate 2008
dc.date.none.fl_str_mv 2008-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/76936
Burgos, Martha Ines; Dassie, Sergio Alberto; Fidelio, Gerardo Daniel; Thermodynamic model for the analysis of calorimetric data of oligomeric proteins; American Chemical Society; Journal of Physical Chemistry B; 112; 45; 12-2008; 14325-14333
1520-6106
1089-5647
CONICET Digital
CONICET
url http://hdl.handle.net/11336/76936
identifier_str_mv Burgos, Martha Ines; Dassie, Sergio Alberto; Fidelio, Gerardo Daniel; Thermodynamic model for the analysis of calorimetric data of oligomeric proteins; American Chemical Society; Journal of Physical Chemistry B; 112; 45; 12-2008; 14325-14333
1520-6106
1089-5647
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/18939789
info:eu-repo/semantics/altIdentifier/doi/10.1021/jp804465c
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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