Utilize este identificador para referenciar este registo:
https://hdl.handle.net/10316/109928
Campo DC | Valor | Idioma |
---|---|---|
dc.contributor.author | Faísca, Patrícia F. N. | - |
dc.contributor.author | Travasso, Rui D. M. | - |
dc.contributor.author | Parisi, Andrea | - |
dc.contributor.author | Rey, Antonio | - |
dc.date.accessioned | 2023-11-07T11:41:25Z | - |
dc.date.available | 2023-11-07T11:41:25Z | - |
dc.date.issued | 2012 | - |
dc.identifier.issn | 1932-6203 | pt |
dc.identifier.uri | http://hdl.handle.net/10316/109928 | - |
dc.description.abstract | For almost 15 years, the experimental correlation between protein folding rates and the contact order parameter has been under scrutiny. Here, we use a simple simulation model combined with a native-centric interaction potential to investigate the physical roots of this empirical observation. We simulate a large set of circular permutants, thus eliminating dependencies of the folding rate on other protein properties (e.g. stability). We show that the rate-contact order correlation is a consequence of the fact that, in high contact order structures, the contact order of the transition state ensemble closely mirrors the contact order of the native state. This happens because, in these structures, the native topology is represented in the transition state through the formation of a network of tertiary interactions that are distinctively long-ranged. | pt |
dc.language.iso | eng | pt |
dc.relation | PTDC/FIS/113638/2009 | pt |
dc.relation | Conselho de Reitores das Universidades Portuguesas (Acção Integrada Luso-Espanhola E-16/09) | pt |
dc.relation | Ministerio de Ciencia e Innovacio´n (FIS2009-13364-C02-02) | pt |
dc.relation | Acción Integrada Hispano-Portuguesa (HP-2008-0065) | pt |
dc.rights | openAccess | pt |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | pt |
dc.subject.mesh | Computer Simulation | pt |
dc.subject.mesh | Kinetics | pt |
dc.subject.mesh | Protein Folding | pt |
dc.subject.mesh | Protein Structure, Tertiary | pt |
dc.subject.mesh | Proteins | pt |
dc.subject.mesh | Thermodynamics | pt |
dc.subject.mesh | Models, Molecular | pt |
dc.title | Why do protein folding rates correlate with metrics of native topology? | pt |
dc.type | article | - |
degois.publication.firstPage | e35599 | pt |
degois.publication.issue | 4 | pt |
degois.publication.title | PLoS ONE | pt |
dc.peerreviewed | yes | pt |
dc.identifier.doi | 10.1371/journal.pone.0035599 | pt |
degois.publication.volume | 7 | pt |
dc.date.embargo | 2012-01-01 | * |
uc.date.periodoEmbargo | 0 | pt |
item.openairetype | article | - |
item.fulltext | Com Texto completo | - |
item.languageiso639-1 | en | - |
item.grantfulltext | open | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
crisitem.author.orcid | 0000-0001-6078-0721 | - |
Aparece nas coleções: | FCTUC Física - Artigos em Revistas Internacionais |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
---|---|---|---|---|
Why-do-protein-folding-rates-correlate-with-metrics-of-native-topologyPLoS-ONE.pdf | 439.97 kB | Adobe PDF | Ver/Abrir |
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