Topology to geometry in protein folding: β-Lactoglobulin

Autores
Fernandez, Ariel; Colubri, Andrés; Berry, Stephen R.
Año de publicación
2000
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Evolution of protein structure from random coil to native is first represented topologically by its time-dependent sequences of discretized Ramachandran basins occupied by successive backbone residues. Introducing energetic and entropic criteria at each instant of observation transforms the description from a structurally ambiguous topological representation to an unambiguous geometric picture of the folding process. The method is applied with success to folding of β-lactoglobulin, traditionally perplexing because of its reputed nonhierarchical folding pattern. This molecule passes through a stage, ca. 0.1 μs duration, of transient, "flickering" α-helical structure, until a bit of tertiary structure forms that stabilizes the system long enough to allow it to pass to its native β-sheet.
Fil: Fernandez, Ariel. University of California; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; Argentina
Fil: Colubri, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; Argentina
Fil: Berry, Stephen R.. University of Chicago; Estados Unidos
Materia
Protein Folding
Cooperativity
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:11336/78536
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Topology to geometry in protein folding: β-LactoglobulinFernandez, ArielColubri, AndrésBerry, Stephen R.Protein FoldingCooperativityhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Evolution of protein structure from random coil to native is first represented topologically by its time-dependent sequences of discretized Ramachandran basins occupied by successive backbone residues. Introducing energetic and entropic criteria at each instant of observation transforms the description from a structurally ambiguous topological representation to an unambiguous geometric picture of the folding process. The method is applied with success to folding of β-lactoglobulin, traditionally perplexing because of its reputed nonhierarchical folding pattern. This molecule passes through a stage, ca. 0.1 μs duration, of transient, "flickering" α-helical structure, until a bit of tertiary structure forms that stabilizes the system long enough to allow it to pass to its native β-sheet.Fil: Fernandez, Ariel. University of California; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; ArgentinaFil: Colubri, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; ArgentinaFil: Berry, Stephen R.. University of Chicago; Estados UnidosNational Academy of Sciences2000-12-19info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/78536Fernandez, Ariel; Colubri, Andrés; Berry, Stephen R.; Topology to geometry in protein folding: β-Lactoglobulin; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 97; 26; 19-12-2000; 14062-140660027-84241091-6490CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/97/26/14062info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.260359997info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:33:39Zoai:ri.conicet.gov.ar:11336/78536instacron: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 09:33:39.829CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Topology to geometry in protein folding: β-Lactoglobulin
title Topology to geometry in protein folding: β-Lactoglobulin
spellingShingle Topology to geometry in protein folding: β-Lactoglobulin
Fernandez, Ariel
Protein Folding
Cooperativity
title_short Topology to geometry in protein folding: β-Lactoglobulin
title_full Topology to geometry in protein folding: β-Lactoglobulin
title_fullStr Topology to geometry in protein folding: β-Lactoglobulin
title_full_unstemmed Topology to geometry in protein folding: β-Lactoglobulin
title_sort Topology to geometry in protein folding: β-Lactoglobulin
dc.creator.none.fl_str_mv Fernandez, Ariel
Colubri, Andrés
Berry, Stephen R.
author Fernandez, Ariel
author_facet Fernandez, Ariel
Colubri, Andrés
Berry, Stephen R.
author_role author
author2 Colubri, Andrés
Berry, Stephen R.
author2_role author
author
dc.subject.none.fl_str_mv Protein Folding
Cooperativity
topic Protein Folding
Cooperativity
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Evolution of protein structure from random coil to native is first represented topologically by its time-dependent sequences of discretized Ramachandran basins occupied by successive backbone residues. Introducing energetic and entropic criteria at each instant of observation transforms the description from a structurally ambiguous topological representation to an unambiguous geometric picture of the folding process. The method is applied with success to folding of β-lactoglobulin, traditionally perplexing because of its reputed nonhierarchical folding pattern. This molecule passes through a stage, ca. 0.1 μs duration, of transient, "flickering" α-helical structure, until a bit of tertiary structure forms that stabilizes the system long enough to allow it to pass to its native β-sheet.
Fil: Fernandez, Ariel. University of California; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; Argentina
Fil: Colubri, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; Argentina
Fil: Berry, Stephen R.. University of Chicago; Estados Unidos
description Evolution of protein structure from random coil to native is first represented topologically by its time-dependent sequences of discretized Ramachandran basins occupied by successive backbone residues. Introducing energetic and entropic criteria at each instant of observation transforms the description from a structurally ambiguous topological representation to an unambiguous geometric picture of the folding process. The method is applied with success to folding of β-lactoglobulin, traditionally perplexing because of its reputed nonhierarchical folding pattern. This molecule passes through a stage, ca. 0.1 μs duration, of transient, "flickering" α-helical structure, until a bit of tertiary structure forms that stabilizes the system long enough to allow it to pass to its native β-sheet.
publishDate 2000
dc.date.none.fl_str_mv 2000-12-19
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/11336/78536
Fernandez, Ariel; Colubri, Andrés; Berry, Stephen R.; Topology to geometry in protein folding: β-Lactoglobulin; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 97; 26; 19-12-2000; 14062-14066
0027-8424
1091-6490
CONICET Digital
CONICET
url http://hdl.handle.net/11336/78536
identifier_str_mv Fernandez, Ariel; Colubri, Andrés; Berry, Stephen R.; Topology to geometry in protein folding: β-Lactoglobulin; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 97; 26; 19-12-2000; 14062-14066
0027-8424
1091-6490
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://www.pnas.org/content/97/26/14062
info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.260359997
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 National Academy of Sciences
publisher.none.fl_str_mv National Academy of Sciences
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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