Ultracompact states of native proteins
- Autores
- Grille Coronel, Leandro; Acierno, Juan Pablo; Ermacora, Mario Roberto
- Año de publicación
- 2017
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- A statistical analysis of circa 20,000 X-ray structures evidenced the effects of temperature of data collection on protein intramolecular distances and degree of compaction. Identical chains with data collected at cryogenic ultralow temperatures (≤160 K) showed a radius of gyration (Rg) significantly smaller than at moderate temperatures (≥240 K). Furthermore, the analysis revealed the existence of structures with a Rg significantly smaller than expected for cryogenic temperatures. In these ultracompact cases, the unusually small Rg could not be specifically attributed to any experimental parameter or crystal features. Ultracompaction involves most atoms and results in their displacement toward the center of the molecule. Ultracompact structures on average have significantly shorter van der Waals and hydrogen bonds than expected for ultralow temperature structures. In addition, the number of van der Waals contacts was larger in ultracompact than in ultralow temperature structures. The structure of these ultracompact states was analyzed in detail and the implication and possible causes of the phenomenon are discussed.
Fil: Grille Coronel, Leandro. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Acierno, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Fil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina - Materia
-
Cryocooling
Protein Compaction
Protein Conformation
Protein Energy Landscape
Protein Glass Transition
Protein Intramolecular Interactions
Radius of Gyration
X-Ray Crystallography - 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:11336/65719
Ver los metadatos del registro completo
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Ultracompact states of native proteinsGrille Coronel, LeandroAcierno, Juan PabloErmacora, Mario RobertoCryocoolingProtein CompactionProtein ConformationProtein Energy LandscapeProtein Glass TransitionProtein Intramolecular InteractionsRadius of GyrationX-Ray Crystallographyhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1A statistical analysis of circa 20,000 X-ray structures evidenced the effects of temperature of data collection on protein intramolecular distances and degree of compaction. Identical chains with data collected at cryogenic ultralow temperatures (≤160 K) showed a radius of gyration (Rg) significantly smaller than at moderate temperatures (≥240 K). Furthermore, the analysis revealed the existence of structures with a Rg significantly smaller than expected for cryogenic temperatures. In these ultracompact cases, the unusually small Rg could not be specifically attributed to any experimental parameter or crystal features. Ultracompaction involves most atoms and results in their displacement toward the center of the molecule. Ultracompact structures on average have significantly shorter van der Waals and hydrogen bonds than expected for ultralow temperature structures. In addition, the number of van der Waals contacts was larger in ultracompact than in ultralow temperature structures. The structure of these ultracompact states was analyzed in detail and the implication and possible causes of the phenomenon are discussed.Fil: Grille Coronel, Leandro. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaFil: Acierno, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; ArgentinaFil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaElsevier Science2017-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/65719Grille Coronel, Leandro; Acierno, Juan Pablo; Ermacora, Mario Roberto; Ultracompact states of native proteins; Elsevier Science; Biophysical Chemistry; 230; 11-2017; 36-440301-4622CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpc.2017.08.004info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0301462217303113info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:37:51Zoai:ri.conicet.gov.ar:11336/65719instacron: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 09:37:51.86CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Ultracompact states of native proteins |
title |
Ultracompact states of native proteins |
spellingShingle |
Ultracompact states of native proteins Grille Coronel, Leandro Cryocooling Protein Compaction Protein Conformation Protein Energy Landscape Protein Glass Transition Protein Intramolecular Interactions Radius of Gyration X-Ray Crystallography |
title_short |
Ultracompact states of native proteins |
title_full |
Ultracompact states of native proteins |
title_fullStr |
Ultracompact states of native proteins |
title_full_unstemmed |
Ultracompact states of native proteins |
title_sort |
Ultracompact states of native proteins |
dc.creator.none.fl_str_mv |
Grille Coronel, Leandro Acierno, Juan Pablo Ermacora, Mario Roberto |
author |
Grille Coronel, Leandro |
author_facet |
Grille Coronel, Leandro Acierno, Juan Pablo Ermacora, Mario Roberto |
author_role |
author |
author2 |
Acierno, Juan Pablo Ermacora, Mario Roberto |
author2_role |
author author |
dc.subject.none.fl_str_mv |
Cryocooling Protein Compaction Protein Conformation Protein Energy Landscape Protein Glass Transition Protein Intramolecular Interactions Radius of Gyration X-Ray Crystallography |
topic |
Cryocooling Protein Compaction Protein Conformation Protein Energy Landscape Protein Glass Transition Protein Intramolecular Interactions Radius of Gyration X-Ray Crystallography |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
A statistical analysis of circa 20,000 X-ray structures evidenced the effects of temperature of data collection on protein intramolecular distances and degree of compaction. Identical chains with data collected at cryogenic ultralow temperatures (≤160 K) showed a radius of gyration (Rg) significantly smaller than at moderate temperatures (≥240 K). Furthermore, the analysis revealed the existence of structures with a Rg significantly smaller than expected for cryogenic temperatures. In these ultracompact cases, the unusually small Rg could not be specifically attributed to any experimental parameter or crystal features. Ultracompaction involves most atoms and results in their displacement toward the center of the molecule. Ultracompact structures on average have significantly shorter van der Waals and hydrogen bonds than expected for ultralow temperature structures. In addition, the number of van der Waals contacts was larger in ultracompact than in ultralow temperature structures. The structure of these ultracompact states was analyzed in detail and the implication and possible causes of the phenomenon are discussed. Fil: Grille Coronel, Leandro. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina Fil: Acierno, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina Fil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina |
description |
A statistical analysis of circa 20,000 X-ray structures evidenced the effects of temperature of data collection on protein intramolecular distances and degree of compaction. Identical chains with data collected at cryogenic ultralow temperatures (≤160 K) showed a radius of gyration (Rg) significantly smaller than at moderate temperatures (≥240 K). Furthermore, the analysis revealed the existence of structures with a Rg significantly smaller than expected for cryogenic temperatures. In these ultracompact cases, the unusually small Rg could not be specifically attributed to any experimental parameter or crystal features. Ultracompaction involves most atoms and results in their displacement toward the center of the molecule. Ultracompact structures on average have significantly shorter van der Waals and hydrogen bonds than expected for ultralow temperature structures. In addition, the number of van der Waals contacts was larger in ultracompact than in ultralow temperature structures. The structure of these ultracompact states was analyzed in detail and the implication and possible causes of the phenomenon are discussed. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-11 |
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/11336/65719 Grille Coronel, Leandro; Acierno, Juan Pablo; Ermacora, Mario Roberto; Ultracompact states of native proteins; Elsevier Science; Biophysical Chemistry; 230; 11-2017; 36-44 0301-4622 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/65719 |
identifier_str_mv |
Grille Coronel, Leandro; Acierno, Juan Pablo; Ermacora, Mario Roberto; Ultracompact states of native proteins; Elsevier Science; Biophysical Chemistry; 230; 11-2017; 36-44 0301-4622 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpc.2017.08.004 info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0301462217303113 |
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 |
Elsevier Science |
publisher.none.fl_str_mv |
Elsevier Science |
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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1844613194709991424 |
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13.070432 |