Configuration-Dependent Diffusion Dynamics of Downhill and Two-State Protein Folding

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorXu, Weixin
dc.creatorLai, Zaizhi
dc.creatorOliveira, Ronaldo J.
dc.creatorLeite, Vitor Barbanti Pereira
dc.creatorWang, Jin
dc.date2014-05-20T14:02:34Z
dc.date2016-10-25T17:09:11Z
dc.date2014-05-20T14:02:34Z
dc.date2016-10-25T17:09:11Z
dc.date2012-05-03
dc.date.accessioned2017-04-05T21:27:56Z
dc.date.available2017-04-05T21:27:56Z
dc.identifierJournal of Physical Chemistry B. Washington: Amer Chemical Soc, v. 116, n. 17, p. 5152-5159, 2012.
dc.identifier1520-6106
dc.identifierhttp://hdl.handle.net/11449/22058
dc.identifierhttp://acervodigital.unesp.br/handle/11449/22058
dc.identifier10.1021/jp212132v
dc.identifierWOS:000303426400006
dc.identifierhttp://dx.doi.org/10.1021/jp212132v
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/867523
dc.descriptionConfiguration-dependent diffusion (CDD) is important for protein folding kinetics with small thermodynamic barriers. CDD can be even more crucial in downhill folding without thermodynamic barriers. We explored the CDD of a downhill protein (BBL), and a two-state protein (CI2). The hidden kinetic barriers due to CDD were revealed. The increased similar to 1 k(B)T kinetic barrier is in line with experimental value based on other fast folding proteins. Compared to that of CI2, the effective free-energy profile of BBL is found to be significantly influenced by CDD, and the kinetics are totally determined by diffusion. These findings are consistent with both earlier bulk and single-molecule fluorescence measurements. In addition, we found the temperature dependence of CDD. We also found that the ratio of folding transition temperature against optimal kinetic folding temperature can provide both a quantitative measure for the underlying landscape topography and an indicator for the possible appearance of downhill folding. Our study can help for a better understanding of the role of diffusion in protein folding dynamics.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageeng
dc.publisherAmer Chemical Soc
dc.relationJournal of Physical Chemistry B
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.titleConfiguration-Dependent Diffusion Dynamics of Downhill and Two-State Protein Folding
dc.typeOtro


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