Folding of small disulfide-rich proteins : clarifying the puzzle

The process by which small proteins fold to their native conformations has been intensively studied over the last few decades. In this field, the particular chemistry of disulfide bond formation has facilitated the characterization of the oxidative folding of numerous small, disulfide-rich proteins...

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Autores: Arolas, Joan L., Ventura, Salvador|||0000-0002-9652-6351, Avilés, Francesc Xavier|||0000-0002-1399-6789, Chang, Jui-Yoa
Formato: artículo
Fecha de publicación:2006
País:España
Recursos:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:67768
Acesso em linha:https://ddd.uab.cat/record/67768
https://dx.doi.org/urn:doi:10.1016/j.tibs.2006.03.005
Access Level:acceso abierto
Palavra-chave:PREI 2008
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spelling Folding of small disulfide-rich proteins : clarifying the puzzleArolas, Joan L.Ventura, Salvador|||0000-0002-9652-6351Avilés, Francesc Xavier|||0000-0002-1399-6789Chang, Jui-YoaPREI 2008The process by which small proteins fold to their native conformations has been intensively studied over the last few decades. In this field, the particular chemistry of disulfide bond formation has facilitated the characterization of the oxidative folding of numerous small, disulfide-rich proteins with results that illustrate a high diversity of folding mechanisms, differing in the heterogeneity and disulfide pairing nativeness of their intermediates. In this review, we combine information on the folding of different protein models together with the recent structural determinations of major intermediates to provide new molecular clues in oxidative folding. Also, we turn to analyze the role of disulfide bonds in misfolding and protein aggregation and their implications in amyloidosis and conformational diseases. 22006-01-0120062006-01-01Articlehttp://purl.org/coar/resource_type/c_6501AMhttp://purl.org/coar/version/c_ab4af688f83e57aainfo:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/67768https://dx.doi.org/urn:doi:10.1016/j.tibs.2006.03.005reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengopen accesshttp://purl.org/coar/access_right/c_abf2Aquest material està protegit per drets d'autor i/o drets afins. Podeu utilitzar aquest material en funció del que permet la legislació de drets d'autor i drets afins d'aplicació al vostre cas. Per a d'altres usos heu d'obtenir permís del(s) titular(s) de drets.https://rightsstatements.org/vocab/InC/1.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:677682026-06-06T12:50:31Z
dc.title.none.fl_str_mv Folding of small disulfide-rich proteins : clarifying the puzzle
title Folding of small disulfide-rich proteins : clarifying the puzzle
spellingShingle Folding of small disulfide-rich proteins : clarifying the puzzle
Arolas, Joan L.
PREI 2008
title_short Folding of small disulfide-rich proteins : clarifying the puzzle
title_full Folding of small disulfide-rich proteins : clarifying the puzzle
title_fullStr Folding of small disulfide-rich proteins : clarifying the puzzle
title_full_unstemmed Folding of small disulfide-rich proteins : clarifying the puzzle
title_sort Folding of small disulfide-rich proteins : clarifying the puzzle
dc.creator.none.fl_str_mv Arolas, Joan L.
Ventura, Salvador|||0000-0002-9652-6351
Avilés, Francesc Xavier|||0000-0002-1399-6789
Chang, Jui-Yoa
author Arolas, Joan L.
author_facet Arolas, Joan L.
Ventura, Salvador|||0000-0002-9652-6351
Avilés, Francesc Xavier|||0000-0002-1399-6789
Chang, Jui-Yoa
author_role author
author2 Ventura, Salvador|||0000-0002-9652-6351
Avilés, Francesc Xavier|||0000-0002-1399-6789
Chang, Jui-Yoa
author2_role author
author
author
dc.subject.none.fl_str_mv PREI 2008
topic PREI 2008
description The process by which small proteins fold to their native conformations has been intensively studied over the last few decades. In this field, the particular chemistry of disulfide bond formation has facilitated the characterization of the oxidative folding of numerous small, disulfide-rich proteins with results that illustrate a high diversity of folding mechanisms, differing in the heterogeneity and disulfide pairing nativeness of their intermediates. In this review, we combine information on the folding of different protein models together with the recent structural determinations of major intermediates to provide new molecular clues in oxidative folding. Also, we turn to analyze the role of disulfide bonds in misfolding and protein aggregation and their implications in amyloidosis and conformational diseases.
publishDate 2006
dc.date.none.fl_str_mv 2
2006-01-01
2006
2006-01-01
dc.type.none.fl_str_mv Article
http://purl.org/coar/resource_type/c_6501
AM
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dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
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https://dx.doi.org/urn:doi:10.1016/j.tibs.2006.03.005
url https://ddd.uab.cat/record/67768
https://dx.doi.org/urn:doi:10.1016/j.tibs.2006.03.005
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
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dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Dipòsit Digital de Documents de la UAB
instname:Universitat Autònoma de Barcelona
instname_str Universitat Autònoma de Barcelona
reponame_str Dipòsit Digital de Documents de la UAB
collection Dipòsit Digital de Documents de la UAB
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