Teaching noncovalent interactions using protein molecular evolution

Autores
Fornasari, Maria Silvina; Parisi, Gustavo Daniel; Echave, Julián
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Noncovalent interactions and physicochemical properties of amino acids are important topics in biochemistry courses. Here, we present a computational laboratory where the capacity of each of the 20 amino acids to maintain different noncovalent interactions are used to investigate the stabilizing forces in a set of proteins coming from organisms adapted to different environments. Using protein sequence and structure information it is possible to evaluate the noncovalent contributions to the stabilization of a given protein fold. As a case study, we use the protein lumazine synthase from three different organisms adapted to live in extreme temperatures: one psychrophilic (optimal growth temperature, 0–20 8C), one mesophilic (optimal growth temperature, 20–50 8C), and one thermophilic (optimal growth temperature, 80–110 8C). We found that this computational laboratory for biochemistry and molecular biology courses enhances student amino acid noncovalent interaction understanding and how these interactions are involved in protein stability.
Fil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Echave, Julián. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina
Materia
EVOLUTION
ADAPTATION
AMINOACIDS
CONSERVATION
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:11336/282235
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Teaching noncovalent interactions using protein molecular evolutionFornasari, Maria SilvinaParisi, Gustavo DanielEchave, JuliánEVOLUTIONADAPTATIONAMINOACIDSCONSERVATIONhttps://purl.org/becyt/ford/1.7https://purl.org/becyt/ford/1Noncovalent interactions and physicochemical properties of amino acids are important topics in biochemistry courses. Here, we present a computational laboratory where the capacity of each of the 20 amino acids to maintain different noncovalent interactions are used to investigate the stabilizing forces in a set of proteins coming from organisms adapted to different environments. Using protein sequence and structure information it is possible to evaluate the noncovalent contributions to the stabilization of a given protein fold. As a case study, we use the protein lumazine synthase from three different organisms adapted to live in extreme temperatures: one psychrophilic (optimal growth temperature, 0–20 8C), one mesophilic (optimal growth temperature, 20–50 8C), and one thermophilic (optimal growth temperature, 80–110 8C). We found that this computational laboratory for biochemistry and molecular biology courses enhances student amino acid noncovalent interaction understanding and how these interactions are involved in protein stability.Fil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Echave, Julián. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; ArgentinaJohn Wiley & Sons2008-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/282235Fornasari, Maria Silvina; Parisi, Gustavo Daniel; Echave, Julián; Teaching noncovalent interactions using protein molecular evolution; John Wiley & Sons; Biochemistry and Molecular Biology Education; 36; 4; 4-2008; 284-2861470-8175CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://iubmb.onlinelibrary.wiley.com/doi/10.1002/bmb.20195info:eu-repo/semantics/altIdentifier/doi/10.1002/bmb.20195info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-03-11T12:27:15Zoai:ri.conicet.gov.ar:11336/282235instacron: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:34982026-03-11 12:27:15.691CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Teaching noncovalent interactions using protein molecular evolution
title Teaching noncovalent interactions using protein molecular evolution
spellingShingle Teaching noncovalent interactions using protein molecular evolution
Fornasari, Maria Silvina
EVOLUTION
ADAPTATION
AMINOACIDS
CONSERVATION
title_short Teaching noncovalent interactions using protein molecular evolution
title_full Teaching noncovalent interactions using protein molecular evolution
title_fullStr Teaching noncovalent interactions using protein molecular evolution
title_full_unstemmed Teaching noncovalent interactions using protein molecular evolution
title_sort Teaching noncovalent interactions using protein molecular evolution
dc.creator.none.fl_str_mv Fornasari, Maria Silvina
Parisi, Gustavo Daniel
Echave, Julián
author Fornasari, Maria Silvina
author_facet Fornasari, Maria Silvina
Parisi, Gustavo Daniel
Echave, Julián
author_role author
author2 Parisi, Gustavo Daniel
Echave, Julián
author2_role author
author
dc.subject.none.fl_str_mv EVOLUTION
ADAPTATION
AMINOACIDS
CONSERVATION
topic EVOLUTION
ADAPTATION
AMINOACIDS
CONSERVATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.7
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Noncovalent interactions and physicochemical properties of amino acids are important topics in biochemistry courses. Here, we present a computational laboratory where the capacity of each of the 20 amino acids to maintain different noncovalent interactions are used to investigate the stabilizing forces in a set of proteins coming from organisms adapted to different environments. Using protein sequence and structure information it is possible to evaluate the noncovalent contributions to the stabilization of a given protein fold. As a case study, we use the protein lumazine synthase from three different organisms adapted to live in extreme temperatures: one psychrophilic (optimal growth temperature, 0–20 8C), one mesophilic (optimal growth temperature, 20–50 8C), and one thermophilic (optimal growth temperature, 80–110 8C). We found that this computational laboratory for biochemistry and molecular biology courses enhances student amino acid noncovalent interaction understanding and how these interactions are involved in protein stability.
Fil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Echave, Julián. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina
description Noncovalent interactions and physicochemical properties of amino acids are important topics in biochemistry courses. Here, we present a computational laboratory where the capacity of each of the 20 amino acids to maintain different noncovalent interactions are used to investigate the stabilizing forces in a set of proteins coming from organisms adapted to different environments. Using protein sequence and structure information it is possible to evaluate the noncovalent contributions to the stabilization of a given protein fold. As a case study, we use the protein lumazine synthase from three different organisms adapted to live in extreme temperatures: one psychrophilic (optimal growth temperature, 0–20 8C), one mesophilic (optimal growth temperature, 20–50 8C), and one thermophilic (optimal growth temperature, 80–110 8C). We found that this computational laboratory for biochemistry and molecular biology courses enhances student amino acid noncovalent interaction understanding and how these interactions are involved in protein stability.
publishDate 2008
dc.date.none.fl_str_mv 2008-04
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/11336/282235
Fornasari, Maria Silvina; Parisi, Gustavo Daniel; Echave, Julián; Teaching noncovalent interactions using protein molecular evolution; John Wiley & Sons; Biochemistry and Molecular Biology Education; 36; 4; 4-2008; 284-286
1470-8175
CONICET Digital
CONICET
url http://hdl.handle.net/11336/282235
identifier_str_mv Fornasari, Maria Silvina; Parisi, Gustavo Daniel; Echave, Julián; Teaching noncovalent interactions using protein molecular evolution; John Wiley & Sons; Biochemistry and Molecular Biology Education; 36; 4; 4-2008; 284-286
1470-8175
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://iubmb.onlinelibrary.wiley.com/doi/10.1002/bmb.20195
info:eu-repo/semantics/altIdentifier/doi/10.1002/bmb.20195
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
application/pdf
dc.publisher.none.fl_str_mv John Wiley & Sons
publisher.none.fl_str_mv John Wiley & Sons
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 12.977003

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