Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli
- Autores
- Villegas, Josefina Maria; Torres Bugeau, Clarisa Maria; Burgos, Martha Ines; Fidelio, Gerardo Daniel; Chehin, Rosana Nieves; Rintoul, Maria Regina; Rapisarda, Viviana Andrea
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- documento de conferencia
- Estado
- versión publicada
- Descripción
- NADH dehydrogenase-2 (NDH-2) of Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.
Fil: Villegas, Josefina Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Torres Bugeau, Clarisa Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Burgos, Martha Ines. 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
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
Fil: Chehin, Rosana Nieves. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Rintoul, Maria Regina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Rapisarda, Viviana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
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ESCHERICHIA COLI - Nivel de accesibilidad
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Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coliVillegas, Josefina MariaTorres Bugeau, Clarisa MariaBurgos, Martha InesFidelio, Gerardo DanielChehin, Rosana NievesRintoul, Maria ReginaRapisarda, Viviana AndreaFADNADHESCHERICHIA COLIhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1NADH dehydrogenase-2 (NDH-2) of Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.Fil: Villegas, Josefina Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Torres Bugeau, Clarisa Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Burgos, Martha Ines. 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; 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; ArgentinaFil: Chehin, Rosana Nieves. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Rintoul, Maria Regina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Rapisarda, Viviana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaXLI Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia MolecularFoz do IguacuBrasilSociedade Brasileira de Bioquímica e Biologia MolecularSociedade Brasileira de Bioquímica e Biologia Molecular2012info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/235545Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli; XLI Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular; Foz do Iguacu; Brasil; 2012; 1-1CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www2.sbbq.org.br/reuniao/cdrom/ra2012/resumos/R9191.pdfInternacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:05:04Zoai:ri.conicet.gov.ar:11336/235545instacron: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:34982025-09-29 10:05:04.94CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli |
title |
Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli |
spellingShingle |
Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli Villegas, Josefina Maria FAD NADH ESCHERICHIA COLI |
title_short |
Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli |
title_full |
Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli |
title_fullStr |
Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli |
title_full_unstemmed |
Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli |
title_sort |
Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli |
dc.creator.none.fl_str_mv |
Villegas, Josefina Maria Torres Bugeau, Clarisa Maria Burgos, Martha Ines Fidelio, Gerardo Daniel Chehin, Rosana Nieves Rintoul, Maria Regina Rapisarda, Viviana Andrea |
author |
Villegas, Josefina Maria |
author_facet |
Villegas, Josefina Maria Torres Bugeau, Clarisa Maria Burgos, Martha Ines Fidelio, Gerardo Daniel Chehin, Rosana Nieves Rintoul, Maria Regina Rapisarda, Viviana Andrea |
author_role |
author |
author2 |
Torres Bugeau, Clarisa Maria Burgos, Martha Ines Fidelio, Gerardo Daniel Chehin, Rosana Nieves Rintoul, Maria Regina Rapisarda, Viviana Andrea |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
FAD NADH ESCHERICHIA COLI |
topic |
FAD NADH ESCHERICHIA COLI |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
NADH dehydrogenase-2 (NDH-2) of Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy. Fil: Villegas, Josefina Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Torres Bugeau, Clarisa Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Burgos, Martha Ines. 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 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 Fil: Chehin, Rosana Nieves. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Rintoul, Maria Regina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Rapisarda, Viviana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina XLI Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular Foz do Iguacu Brasil Sociedade Brasileira de Bioquímica e Biologia Molecular |
description |
NADH dehydrogenase-2 (NDH-2) of Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012 |
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info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/conferenceObject Reunión Book http://purl.org/coar/resource_type/c_5794 info:ar-repo/semantics/documentoDeConferencia |
status_str |
publishedVersion |
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conferenceObject |
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http://hdl.handle.net/11336/235545 Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli; XLI Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular; Foz do Iguacu; Brasil; 2012; 1-1 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/235545 |
identifier_str_mv |
Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli; XLI Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular; Foz do Iguacu; Brasil; 2012; 1-1 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://www2.sbbq.org.br/reuniao/cdrom/ra2012/resumos/R9191.pdf |
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info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
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openAccess |
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Internacional |
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Sociedade Brasileira de Bioquímica e Biologia Molecular |
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Sociedade Brasileira de Bioquímica e Biologia Molecular |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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