Estudio de Dinamica de Agregacion proteica con TRP-Cage

Autores
Faundez, Cristian Leonel; Meyra, Ariel German; Ferrara, Carlos Gaston
Año de publicación
2018
Idioma
español castellano
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We studied by molecular dynamics (MD) aggregating two mini proteins such as TRP-cage (TRP) in neutral pH conditions and with explicit solvent. The results correspond to two different systems, the first with 3952 water molecules and one TRP and the second with 7654 water molecules and two TRPs. Both systems were simulated in NVT and NPT ensembles, with T = 300 K and P = 1 bar. The results show the formation of stable dimers in short simulation times. The analyzes made from the surface accessible to the solvent show that the main mechanism or driver of the formation of these dimers at neutral pH is the hydrophobic interaction between different sectors of the protein (hydrophobic amino acids). Keywords: Proteins,TRP-cage,Solvent Accessible Surface(SASA).

Fil: Faundez, Cristian Leonel. Universidad Nacional Arturo Jauretche; Argentina
Fil: Meyra, Ariel German. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Ferrara, Carlos Gaston. Universidad Nacional Arturo Jauretche; Argentina
Materia
AGREGACION DE PROTEINAS
SIMULACION
DINAMICA MOLECULAR
TRP-CAGE
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:11336/89284
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Estudio de Dinamica de Agregacion proteica con TRP-CageFaundez, Cristian LeonelMeyra, Ariel GermanFerrara, Carlos GastonAGREGACION DE PROTEINASSIMULACIONDINAMICA MOLECULARTRP-CAGEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We studied by molecular dynamics (MD) aggregating two mini proteins such as TRP-cage (TRP) in neutral pH conditions and with explicit solvent. The results correspond to two different systems, the first with 3952 water molecules and one TRP and the second with 7654 water molecules and two TRPs. Both systems were simulated in NVT and NPT ensembles, with T = 300 K and P = 1 bar. The results show the formation of stable dimers in short simulation times. The analyzes made from the surface accessible to the solvent show that the main mechanism or driver of the formation of these dimers at neutral pH is the hydrophobic interaction between different sectors of the protein (hydrophobic amino acids). Keywords: Proteins,TRP-cage,Solvent Accessible Surface(SASA).<br />Fil: Faundez, Cristian Leonel. Universidad Nacional Arturo Jauretche; ArgentinaFil: Meyra, Ariel German. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; ArgentinaFil: Ferrara, Carlos Gaston. Universidad Nacional Arturo Jauretche; ArgentinaUNIPAZ2018-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/89284Faundez, Cristian Leonel; Meyra, Ariel German; Ferrara, Carlos Gaston; Estudio de Dinamica de Agregacion proteica con TRP-Cage; UNIPAZ; Ciencia Tecnologia Sociedad y Ambiente; 10; 15; 7-2018; 17-222027 6745CONICET DigitalCONICETspainfo:eu-repo/semantics/altIdentifier/url/http://www.unipaz.edu.co/ojs/index.php/revcitecsa/article/view/165/pdfinfo:eu-repo/semantics/altIdentifier/url/https://unipaz.edu.co/ojs/index.php/revcitecsa/issue/view/2017-6745info:eu-repo/semantics/altIdentifier/url/https://unipaz.edu.co/ojs/index.php/revcitecsa/issue/view/2017-6745/showTocinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:02:05Zoai:ri.conicet.gov.ar:11336/89284instacron: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 10:02:05.673CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Estudio de Dinamica de Agregacion proteica con TRP-Cage
title Estudio de Dinamica de Agregacion proteica con TRP-Cage
spellingShingle Estudio de Dinamica de Agregacion proteica con TRP-Cage
Faundez, Cristian Leonel
AGREGACION DE PROTEINAS
SIMULACION
DINAMICA MOLECULAR
TRP-CAGE
title_short Estudio de Dinamica de Agregacion proteica con TRP-Cage
title_full Estudio de Dinamica de Agregacion proteica con TRP-Cage
title_fullStr Estudio de Dinamica de Agregacion proteica con TRP-Cage
title_full_unstemmed Estudio de Dinamica de Agregacion proteica con TRP-Cage
title_sort Estudio de Dinamica de Agregacion proteica con TRP-Cage
dc.creator.none.fl_str_mv Faundez, Cristian Leonel
Meyra, Ariel German
Ferrara, Carlos Gaston
author Faundez, Cristian Leonel
author_facet Faundez, Cristian Leonel
Meyra, Ariel German
Ferrara, Carlos Gaston
author_role author
author2 Meyra, Ariel German
Ferrara, Carlos Gaston
author2_role author
author
dc.subject.none.fl_str_mv AGREGACION DE PROTEINAS
SIMULACION
DINAMICA MOLECULAR
TRP-CAGE
topic AGREGACION DE PROTEINAS
SIMULACION
DINAMICA MOLECULAR
TRP-CAGE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv We studied by molecular dynamics (MD) aggregating two mini proteins such as TRP-cage (TRP) in neutral pH conditions and with explicit solvent. The results correspond to two different systems, the first with 3952 water molecules and one TRP and the second with 7654 water molecules and two TRPs. Both systems were simulated in NVT and NPT ensembles, with T = 300 K and P = 1 bar. The results show the formation of stable dimers in short simulation times. The analyzes made from the surface accessible to the solvent show that the main mechanism or driver of the formation of these dimers at neutral pH is the hydrophobic interaction between different sectors of the protein (hydrophobic amino acids). Keywords: Proteins,TRP-cage,Solvent Accessible Surface(SASA).<br />
Fil: Faundez, Cristian Leonel. Universidad Nacional Arturo Jauretche; Argentina
Fil: Meyra, Ariel German. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Ferrara, Carlos Gaston. Universidad Nacional Arturo Jauretche; Argentina
description We studied by molecular dynamics (MD) aggregating two mini proteins such as TRP-cage (TRP) in neutral pH conditions and with explicit solvent. The results correspond to two different systems, the first with 3952 water molecules and one TRP and the second with 7654 water molecules and two TRPs. Both systems were simulated in NVT and NPT ensembles, with T = 300 K and P = 1 bar. The results show the formation of stable dimers in short simulation times. The analyzes made from the surface accessible to the solvent show that the main mechanism or driver of the formation of these dimers at neutral pH is the hydrophobic interaction between different sectors of the protein (hydrophobic amino acids). Keywords: Proteins,TRP-cage,Solvent Accessible Surface(SASA).<br />
publishDate 2018
dc.date.none.fl_str_mv 2018-07
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/11336/89284
Faundez, Cristian Leonel; Meyra, Ariel German; Ferrara, Carlos Gaston; Estudio de Dinamica de Agregacion proteica con TRP-Cage; UNIPAZ; Ciencia Tecnologia Sociedad y Ambiente; 10; 15; 7-2018; 17-22
2027 6745
CONICET Digital
CONICET
url http://hdl.handle.net/11336/89284
identifier_str_mv Faundez, Cristian Leonel; Meyra, Ariel German; Ferrara, Carlos Gaston; Estudio de Dinamica de Agregacion proteica con TRP-Cage; UNIPAZ; Ciencia Tecnologia Sociedad y Ambiente; 10; 15; 7-2018; 17-22
2027 6745
CONICET Digital
CONICET
dc.language.none.fl_str_mv spa
language spa
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.unipaz.edu.co/ojs/index.php/revcitecsa/article/view/165/pdf
info:eu-repo/semantics/altIdentifier/url/https://unipaz.edu.co/ojs/index.php/revcitecsa/issue/view/2017-6745
info:eu-repo/semantics/altIdentifier/url/https://unipaz.edu.co/ojs/index.php/revcitecsa/issue/view/2017-6745/showToc
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
dc.publisher.none.fl_str_mv UNIPAZ
publisher.none.fl_str_mv UNIPAZ
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 13.070432

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