Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme

Autores
Gutiérrez, Lucas J.; Enriz, Ricardo Daniel; Baldoni, Hector Armando
Año de publicación
2012
Idioma
inglés
Tipo de recurso
parte de libro
Estado
versión publicada
Descripción
Proteins and enzymes poses a non-covalent 3D structure and therefore their intrinsic flexibility allows the existence of an ensemble of different conformers which are separated by a low-energy barrier. These ranges of available conformers for proteins in solution are due to the relative movements among the different domains. Domain motions are important for a variety of protein functions, including catalysis, regulation of activity, transport of metabolites, formation of protein assemblies, and cellular locomotion. Considering the importance of these conformational changes it is obvious that the different techniques to evaluate these behaviours are very important in order to understand the biological effects. In the present chapter we report molecular dynamics (MD) trajectories analyzed by essential dynamics method on three different molecular systems of biological interest: i) DNA-bending protein Fis (Factor for Inversion Stimulation), ii) DNA-tvMyb1 (Trichomonas vaginalis transcriptional factor) and iii) the BACE1 (beta site amyloid cleaving enzyme 1). Although the general structural characteristics for the above systems are well known, comparatively little information is available about their flexibility and dynamics. This is in part due to difficulties with obtaining such information experimentally. Thus, our primary interest was the comparison between the unligated and the complexed state, because the corresponding conclusions may reveal motions of functional relevance.
Fil: Gutiérrez, Lucas J.. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Área Química General e Inorgánica; Argentina
Fil: Enriz, Ricardo Daniel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Área Química General e Inorgánica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Baldoni, Hector Armando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi". Universidad Nacional de San Luis. Facultad de Ciencias Físico, Matemáticas y Naturales. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi"; Argentina
Materia
ESSENTIAL DYNAMICS
BENDING PROTEINS
TRANSCRIPTIONAL FACTORS
BACE1
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:11336/242425
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/242425
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzymeGutiérrez, Lucas J.Enriz, Ricardo DanielBaldoni, Hector ArmandoESSENTIAL DYNAMICSBENDING PROTEINSTRANSCRIPTIONAL FACTORSBACE1https://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Proteins and enzymes poses a non-covalent 3D structure and therefore their intrinsic flexibility allows the existence of an ensemble of different conformers which are separated by a low-energy barrier. These ranges of available conformers for proteins in solution are due to the relative movements among the different domains. Domain motions are important for a variety of protein functions, including catalysis, regulation of activity, transport of metabolites, formation of protein assemblies, and cellular locomotion. Considering the importance of these conformational changes it is obvious that the different techniques to evaluate these behaviours are very important in order to understand the biological effects. In the present chapter we report molecular dynamics (MD) trajectories analyzed by essential dynamics method on three different molecular systems of biological interest: i) DNA-bending protein Fis (Factor for Inversion Stimulation), ii) DNA-tvMyb1 (Trichomonas vaginalis transcriptional factor) and iii) the BACE1 (beta site amyloid cleaving enzyme 1). Although the general structural characteristics for the above systems are well known, comparatively little information is available about their flexibility and dynamics. This is in part due to difficulties with obtaining such information experimentally. Thus, our primary interest was the comparison between the unligated and the complexed state, because the corresponding conclusions may reveal motions of functional relevance.Fil: Gutiérrez, Lucas J.. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Área Química General e Inorgánica; ArgentinaFil: Enriz, Ricardo Daniel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Área Química General e Inorgánica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Baldoni, Hector Armando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi". Universidad Nacional de San Luis. Facultad de Ciencias Físico, Matemáticas y Naturales. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi"; ArgentinaIntechOpenLichang Wang2012info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/bookParthttp://purl.org/coar/resource_type/c_3248info:ar-repo/semantics/parteDeLibroapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/242425Gutiérrez, Lucas J.; Enriz, Ricardo Daniel; Baldoni, Hector Armando; Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme; IntechOpen; 2012; 151-170978-953-51-0444-5CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.intechopen.com/books/molecular-dynamics-studies-of-synthetic-and-biological-macromoleculesinfo:eu-repo/semantics/altIdentifier/doi/10.5772/36506info:eu-repo/semantics/altIdentifier/url/https://www.intechopen.com/chapters/35488info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:02:55Zoai:ri.conicet.gov.ar:11336/242425instacron: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 11:02:56.075CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme
title Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme
spellingShingle Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme
Gutiérrez, Lucas J.
ESSENTIAL DYNAMICS
BENDING PROTEINS
TRANSCRIPTIONAL FACTORS
BACE1
title_short Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme
title_full Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme
title_fullStr Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme
title_full_unstemmed Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme
title_sort Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme
dc.creator.none.fl_str_mv Gutiérrez, Lucas J.
Enriz, Ricardo Daniel
Baldoni, Hector Armando
author Gutiérrez, Lucas J.
author_facet Gutiérrez, Lucas J.
Enriz, Ricardo Daniel
Baldoni, Hector Armando
author_role author
author2 Enriz, Ricardo Daniel
Baldoni, Hector Armando
author2_role author
author
dc.contributor.none.fl_str_mv Lichang Wang
dc.subject.none.fl_str_mv ESSENTIAL DYNAMICS
BENDING PROTEINS
TRANSCRIPTIONAL FACTORS
BACE1
topic ESSENTIAL DYNAMICS
BENDING PROTEINS
TRANSCRIPTIONAL FACTORS
BACE1
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Proteins and enzymes poses a non-covalent 3D structure and therefore their intrinsic flexibility allows the existence of an ensemble of different conformers which are separated by a low-energy barrier. These ranges of available conformers for proteins in solution are due to the relative movements among the different domains. Domain motions are important for a variety of protein functions, including catalysis, regulation of activity, transport of metabolites, formation of protein assemblies, and cellular locomotion. Considering the importance of these conformational changes it is obvious that the different techniques to evaluate these behaviours are very important in order to understand the biological effects. In the present chapter we report molecular dynamics (MD) trajectories analyzed by essential dynamics method on three different molecular systems of biological interest: i) DNA-bending protein Fis (Factor for Inversion Stimulation), ii) DNA-tvMyb1 (Trichomonas vaginalis transcriptional factor) and iii) the BACE1 (beta site amyloid cleaving enzyme 1). Although the general structural characteristics for the above systems are well known, comparatively little information is available about their flexibility and dynamics. This is in part due to difficulties with obtaining such information experimentally. Thus, our primary interest was the comparison between the unligated and the complexed state, because the corresponding conclusions may reveal motions of functional relevance.
Fil: Gutiérrez, Lucas J.. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Área Química General e Inorgánica; Argentina
Fil: Enriz, Ricardo Daniel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Área Química General e Inorgánica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Baldoni, Hector Armando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi". Universidad Nacional de San Luis. Facultad de Ciencias Físico, Matemáticas y Naturales. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi"; Argentina
description Proteins and enzymes poses a non-covalent 3D structure and therefore their intrinsic flexibility allows the existence of an ensemble of different conformers which are separated by a low-energy barrier. These ranges of available conformers for proteins in solution are due to the relative movements among the different domains. Domain motions are important for a variety of protein functions, including catalysis, regulation of activity, transport of metabolites, formation of protein assemblies, and cellular locomotion. Considering the importance of these conformational changes it is obvious that the different techniques to evaluate these behaviours are very important in order to understand the biological effects. In the present chapter we report molecular dynamics (MD) trajectories analyzed by essential dynamics method on three different molecular systems of biological interest: i) DNA-bending protein Fis (Factor for Inversion Stimulation), ii) DNA-tvMyb1 (Trichomonas vaginalis transcriptional factor) and iii) the BACE1 (beta site amyloid cleaving enzyme 1). Although the general structural characteristics for the above systems are well known, comparatively little information is available about their flexibility and dynamics. This is in part due to difficulties with obtaining such information experimentally. Thus, our primary interest was the comparison between the unligated and the complexed state, because the corresponding conclusions may reveal motions of functional relevance.
publishDate 2012
dc.date.none.fl_str_mv 2012
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/bookPart
http://purl.org/coar/resource_type/c_3248
info:ar-repo/semantics/parteDeLibro
status_str publishedVersion
format bookPart
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/242425
Gutiérrez, Lucas J.; Enriz, Ricardo Daniel; Baldoni, Hector Armando; Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme; IntechOpen; 2012; 151-170
978-953-51-0444-5
CONICET Digital
CONICET
url http://hdl.handle.net/11336/242425
identifier_str_mv Gutiérrez, Lucas J.; Enriz, Ricardo Daniel; Baldoni, Hector Armando; Essential dynamics on different biological systems: DNA-bending protein Fis, DNA-tvMyb1 transcriptional factor and BACE1 enzyme; IntechOpen; 2012; 151-170
978-953-51-0444-5
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.intechopen.com/books/molecular-dynamics-studies-of-synthetic-and-biological-macromolecules
info:eu-repo/semantics/altIdentifier/doi/10.5772/36506
info:eu-repo/semantics/altIdentifier/url/https://www.intechopen.com/chapters/35488
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 IntechOpen
publisher.none.fl_str_mv IntechOpen
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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