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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/242425
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T09:34:53Zoai: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:34982025-09-29 09:34:53.995CONICET 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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13.070432 |