Statistical evidence for a helical nascent chain

Detalhes bibliográficos
Autor(a) principal: Cruzeiro, Leonor
Data de Publicação: 2021
Outros Autores: Gill, Andrew C., Eilbeck, J. Chris
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.1/15399
Resumo: We investigate the hypothesis that protein folding is a kinetic, non-equilibrium process, in which the structure of the nascent chain is crucial. We compare actual amino acid frequencies in loops, alpha-helices and beta-sheets with the frequencies that would arise in the absence of any amino acid bias for those secondary structures. The novel analysis suggests that while specific amino acids exist to drive the formation of loops and sheets, none stand out as drivers for alpha-helices. This favours the idea that the alpha-helix is the initial structure of most proteins before the folding process begins.
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spelling Statistical evidence for a helical nascent chainProtein foldingSingle amino acid distributionsFolding pathwayWe investigate the hypothesis that protein folding is a kinetic, non-equilibrium process, in which the structure of the nascent chain is crucial. We compare actual amino acid frequencies in loops, alpha-helices and beta-sheets with the frequencies that would arise in the absence of any amino acid bias for those secondary structures. The novel analysis suggests that while specific amino acids exist to drive the formation of loops and sheets, none stand out as drivers for alpha-helices. This favours the idea that the alpha-helix is the initial structure of most proteins before the folding process begins.UIDB/04326/2020MDPISapientiaCruzeiro, LeonorGill, Andrew C.Eilbeck, J. Chris2021-04-16T13:30:42Z2021-02-262021-03-26T14:06:15Z2021-02-26T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/15399engBiomolecules 11 (3): 357 (2021)10.3390/biom11030357info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-24T10:27:43ZPortal AgregadorONG
dc.title.none.fl_str_mv Statistical evidence for a helical nascent chain
title Statistical evidence for a helical nascent chain
spellingShingle Statistical evidence for a helical nascent chain
Cruzeiro, Leonor
Protein folding
Single amino acid distributions
Folding pathway
title_short Statistical evidence for a helical nascent chain
title_full Statistical evidence for a helical nascent chain
title_fullStr Statistical evidence for a helical nascent chain
title_full_unstemmed Statistical evidence for a helical nascent chain
title_sort Statistical evidence for a helical nascent chain
author Cruzeiro, Leonor
author_facet Cruzeiro, Leonor
Gill, Andrew C.
Eilbeck, J. Chris
author_role author
author2 Gill, Andrew C.
Eilbeck, J. Chris
author2_role author
author
dc.contributor.none.fl_str_mv Sapientia
dc.contributor.author.fl_str_mv Cruzeiro, Leonor
Gill, Andrew C.
Eilbeck, J. Chris
dc.subject.por.fl_str_mv Protein folding
Single amino acid distributions
Folding pathway
topic Protein folding
Single amino acid distributions
Folding pathway
description We investigate the hypothesis that protein folding is a kinetic, non-equilibrium process, in which the structure of the nascent chain is crucial. We compare actual amino acid frequencies in loops, alpha-helices and beta-sheets with the frequencies that would arise in the absence of any amino acid bias for those secondary structures. The novel analysis suggests that while specific amino acids exist to drive the formation of loops and sheets, none stand out as drivers for alpha-helices. This favours the idea that the alpha-helix is the initial structure of most proteins before the folding process begins.
publishDate 2021
dc.date.none.fl_str_mv 2021-04-16T13:30:42Z
2021-02-26
2021-03-26T14:06:15Z
2021-02-26T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.1/15399
url http://hdl.handle.net/10400.1/15399
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Biomolecules 11 (3): 357 (2021)
10.3390/biom11030357
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
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